{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRab11A is emerging as a master regulator of polarized membrane trafficking. It orchestrates the delivery of specific cargo from recycling endosomes to distinct plasma membrane domains, a process central to the biogenesis of primary cilia through the targeted recruitment of Rabin8 and subsequent Rab8 activation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In addition, Rab11A‐dependent vesicular transport from recycling endosomes contributes to autophagosome formation under starvation, and mediates receptor recycling events – including that of transferrin and receptor tyrosine kinases – often in coordination with myosin Vb and other effector proteins."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "3", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRab11A also plays a crucial role in the life cycle of several viruses. In influenza A virus–infected cells, for example, Rab11A associates with viral ribonucleoprotein (vRNP) complexes to facilitate their transit from the nucleus to the plasma membrane, a pathway essential for proper virion morphogenesis and filament formation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its functions in epithelial and viral contexts, Rab11A regulates endosomal sorting in immune and host defense responses. It directs the transport of Toll-like receptor 4 and its adaptor molecules to phagosomes during bacterial infections and is recruited early at the site of invasion by Shigella to facilitate vacuolar membrane rupture, a step critical for pathogen escape."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": " Moreover, interactions between Rab11A and G protein βγ subunits support the assembly of signaling complexes on endosomes that lead to PI3K activation and subsequent AKT phosphorylation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nStructural and cell‐biological studies further underscore Rab11A’s central role in the spatial control of vesicle trafficking. Crystal‐structure analyses have revealed conformational features that support its ability to engage distinct effector proteins, while in dividing cells Rab11A accumulates at the cleavage furrow and midbody to ensure the final stages of cytokinesis. Additionally, the dynamic interplay between Rab11A and members of the Rab11–FIP family – as well as with regulators such as Rabin8 – organizes discrete subdomains that promote both recycling and abscission."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRab11A‐dependent pathways have significant implications for disease. In neurons, Rab11A regulates the resecretion of alpha‐synuclein, thereby reducing aggregation and neurotoxicity, and its role in controlling β‐secretase recycling may influence amyloid‐β production linked to Alzheimer’s disease. In polarized epithelial cells, Rab11A directs trafficking of ABC transporters critical for canalicular formation and supports the maintenance of apical microvilli. Aberrant Rab11A expression is also linked to oncogenic processes, as seen in non–small cell lung cancer, where its upregulation is associated with advanced stage and poor prognosis; in prion disease models, altered Rab11A function correlates with deficits in post–Golgi trafficking."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRab11A also influences the trafficking and signaling of G protein–coupled receptors and other membrane proteins. It plays a role in the recycling of β2-adrenergic receptors from early endosomes through the pericentriolar recycling compartment and modulates vesicle docking/fusion mechanisms that are essential for proper receptor resensitization. In addition, Rab11A is implicated in controlling the dynamics of endocytic recycling during epithelial–mesenchymal transitions and in coordinating receptor signaling in immunological synapse formation, thereby impacting both cell migration and intercellular communication."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, Rab11A contributes to the fine-tuning of receptor signaling cascades that regulate endocrine functions. For example, in cells expressing the calcium-sensing receptor, Rab11A-dependent recycling is vital for the regulated secretion of parathyroid hormone–related peptides, while alterations in Rab11A interactions with PDZ domain proteins such as PICK1 can impact the intracellular trafficking and recycling kinetics of G protein–coupled receptors."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Andreas Knödler, Shanshan Feng, Jian Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Coordination of Rab8 and Rab11 in primary ciliogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1002401107"}], "href": "https://doi.org/10.1073/pnas.1002401107"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20308558"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20308558"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Christopher J Westlake, Lisa M Baye, Maxence V Nachury, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Primary cilia membrane assembly is initiated by Rab11 and transport protein particle II (TRAPPII) complex-dependent trafficking of Rabin8 to the centrosome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1018823108"}], "href": "https://doi.org/10.1073/pnas.1018823108"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21273506"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21273506"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Andrea Longatti, Christopher A Lamb, Minoo Razi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.201111079"}], "href": "https://doi.org/10.1083/jcb.201111079"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22613832"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22613832"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Senye Takahashi, Keiji Kubo, Satoshi Waguri, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rab11 regulates exocytosis of recycling vesicles at the plasma membrane."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.102913"}], "href": "https://doi.org/10.1242/jcs.102913"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22685325"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22685325"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Joseph T Roland, David M Bryant, Anirban Datta, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1010754108"}], "href": "https://doi.org/10.1073/pnas.1010754108"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21282656"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21282656"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Kurt Ballmer-Hofer, Anneli E Andersson, Laura E Ratcliffe, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2011-01-328773"}], "href": "https://doi.org/10.1182/blood-2011-01-328773"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21586748"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21586748"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Maria Joao Amorim, Emily A Bruce, Eliot K C Read, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A Rab11- and microtubule-dependent mechanism for cytoplasmic transport of influenza A virus viral RNA."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.02606-10"}], "href": "https://doi.org/10.1128/JVI.02606-10"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21307188"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21307188"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Emily A Bruce, Paul Digard, Amanda D Stuart "}, {"type": "b", "children": [{"type": "t", "text": "The Rab11 pathway is required for influenza A virus budding and filament formation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.00307-10"}], "href": "https://doi.org/10.1128/JVI.00307-10"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20357086"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20357086"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Amie J Eisfeld, Eiryo Kawakami, Tokiko Watanabe, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RAB11A is essential for transport of the influenza virus genome to the plasma membrane."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.00378-11"}], "href": "https://doi.org/10.1128/JVI.00378-11"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21525351"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21525351"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Eric Nturibi, Amar R Bhagwat, Stefanie Coburn, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Intracellular Colocalization of Influenza Viral RNA and Rab11A Is Dependent upon Microtubule Filaments."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.01179-17"}], "href": "https://doi.org/10.1128/JVI.01179-17"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28724771"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28724771"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Isabel Fernández de Castro Martin, Guillaume Fournier, Martin Sachse, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Influenza virus genome reaches the plasma membrane via a modified endoplasmic reticulum and Rab11-dependent vesicles."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-017-01557-6"}], "href": "https://doi.org/10.1038/s41467-017-01557-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29123131"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29123131"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Harald Husebye, Marie Hjelmseth Aune, Jørgen Stenvik, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Rab11a GTPase controls Toll-like receptor 4-induced activation of interferon regulatory factor-3 on phagosomes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Immunity (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.immuni.2010.09.010"}], "href": "https://doi.org/10.1016/j.immuni.2010.09.010"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20933442"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20933442"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Nora Mellouk, Allon Weiner, Nathalie Aulner, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Shigella subverts the host recycling compartment to rupture its vacuole."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Host Microbe (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.chom.2014.09.005"}], "href": "https://doi.org/10.1016/j.chom.2014.09.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25299335"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25299335"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Alejandro García-Regalado, María Luisa Guzmán-Hernández, Iliana Ramírez-Rangel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "G protein-coupled receptor-promoted trafficking of Gbeta1gamma2 leads to AKT activation at endosomes via a mechanism mediated by Gbeta1gamma2-Rab11a interaction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.e07-10-1089"}], "href": "https://doi.org/10.1091/mbc.e07-10-1089"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18701709"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18701709"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Yoshiyuki Wakabayashi, Parmesh Dutt, Jennifer Lippincott-Schwartz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rab11a and myosin Vb are required for bile canalicular formation in WIF-B9 cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0503702102"}], "href": "https://doi.org/10.1073/pnas.0503702102"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16214890"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16214890"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Xinzi Yu, Rytis Prekeris, Gwyn W Gould "}, {"type": "b", "children": [{"type": "t", "text": "Role of endosomal Rab GTPases in cytokinesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Cell Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ejcb.2006.10.002"}], "href": "https://doi.org/10.1016/j.ejcb.2006.10.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17157409"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17157409"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Melanie Vetter, Ralf Stehle, Claire Basquin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structure of Rab11-FIP3-Rabin8 reveals simultaneous binding of FIP3 and Rabin8 effectors to Rab11."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Struct Mol Biol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nsmb.3065"}], "href": "https://doi.org/10.1038/nsmb.3065"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26258637"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26258637"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Nicholas W Baetz, James R Goldenring "}, {"type": "b", "children": [{"type": "t", "text": "Rab11-family interacting proteins define spatially and temporally distinct regions within the dynamic Rab11a-dependent recycling system."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.E12-09-0659"}], "href": "https://doi.org/10.1091/mbc.E12-09-0659"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23283983"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23283983"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Jun Liu, Jian-Peng Zhang, Min Shi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rab11a and HSP90 regulate recycling of extracellular alpha-synuclein."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurosci (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1523/JNEUROSCI.6202-08.2009"}], "href": "https://doi.org/10.1523/JNEUROSCI.6202-08.2009"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19193894"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19193894"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Vinod Udayar, Virginie Buggia-Prévot, Rita L Guerreiro, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A paired RNAi and RabGAP overexpression screen identifies Rab11 as a regulator of β-amyloid production."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Rep (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.celrep.2013.12.005"}], "href": "https://doi.org/10.1016/j.celrep.2013.12.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24373285"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24373285"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Agnieszka Swiatecka-Urban, Laleh Talebian, Eiko Kanno, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M608531200"}], "href": "https://doi.org/10.1074/jbc.M608531200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17462998"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17462998"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Byron C Knowles, Victoria G Weis, Shiyan Yu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rab11a regulates syntaxin 3 localization and microvillus assembly in enterocytes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.163303"}], "href": "https://doi.org/10.1242/jcs.163303"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25673875"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25673875"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Qianze Dong, Lin Fu, Yue Zhao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rab11a promotes proliferation and invasion through regulation of YAP in non-small cell lung cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.15359"}], "href": "https://doi.org/10.18632/oncotarget.15359"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28468127"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28468127"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Tania Massignan, Emiliano Biasini, Eliana Lauranzano, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutant prion protein expression is associated with an alteration of the Rab GDP dissociation inhibitor alpha (GDI)/Rab11 pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Proteomics (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/mcp.M900271-MCP200"}], "href": "https://doi.org/10.1074/mcp.M900271-MCP200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19996123"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19996123"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Herschel S Dhekne, Nai-Hua Hsiao, Pieter Roelofs, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Myosin Vb and Rab11a regulate phosphorylation of ezrin in enterocytes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.137273"}], "href": "https://doi.org/10.1242/jcs.137273"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24413175"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24413175"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Robert H Moore, Ellen E Millman, Estrella Alpizar-Foster, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rab11 regulates the recycling and lysosome targeting of beta2-adrenergic receptors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.01168"}], "href": "https://doi.org/10.1242/jcs.01168"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15190120"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15190120"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Puneet Khandelwal, Wily G Ruiz, Elena Balestreire-Hawryluk, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rab11a-dependent exocytosis of discoidal/fusiform vesicles in bladder umbrella cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0805636105"}], "href": "https://doi.org/10.1073/pnas.0805636105"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18843107"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18843107"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Melissa L Fowler, Jacob A McPhail, Meredith L Jenkins, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Using hydrogen deuterium exchange mass spectrometry to engineer optimized constructs for crystallization of protein complexes: Case study of PI4KIIIβ with Rab11."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Protein Sci (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/pro.2879"}], "href": "https://doi.org/10.1002/pro.2879"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26756197"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26756197"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Jérôme Bouchet, Iratxe Del Río-Iñiguez, Rémi Lasserre, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rac1-Rab11-FIP3 regulatory hub coordinates vesicle traffic with actin remodeling and T-cell activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.15252/embj.201593274"}], "href": "https://doi.org/10.15252/embj.201593274"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27154205"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27154205"}]}, {"type": "r", "ref": 30, "children": [{"type": "t", "text": "Véronik Lachance, Jade Degrandmaison, Sébastien Marois, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ubiquitylation and activation of a Rab GTPase is promoted by a β₂AR-HACE1 complex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.132944"}], "href": "https://doi.org/10.1242/jcs.132944"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24190883"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24190883"}]}, {"type": "r", "ref": 31, "children": [{"type": "t", "text": "Yuan-Chiang Chung, Wan-Chen Wei, Chia-Nung Hung, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rab11 collaborates E-cadherin to promote collective cell migration and indicates a poor prognosis in colorectal carcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Clin Invest (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/eci.12683"}], "href": "https://doi.org/10.1111/eci.12683"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27696383"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27696383"}]}, {"type": "r", "ref": 32, "children": [{"type": "t", "text": "Emily A Bruce, Amanda Stuart, Mary W McCaffrey, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Role of the Rab11 pathway in negative-strand virus assembly."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Soc Trans (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BST20120166"}], "href": "https://doi.org/10.1042/BST20120166"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23176490"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23176490"}]}, {"type": "r", "ref": 33, "children": [{"type": "t", "text": "Yuan-Chiang Chung, Wan-Chen Wei, Shin-Han Huang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Rab11 regulates E-cadherin expression and induces cell transformation in colorectal carcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Cancer (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1471-2407-14-587"}], "href": "https://doi.org/10.1186/1471-2407-14-587"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25117932"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25117932"}]}, {"type": "r", "ref": 34, "children": [{"type": "t", "text": "Alma P Reyes-Ibarra, Alejandro García-Regalado, Iliana Ramírez-Rangel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Calcium-sensing receptor endocytosis links extracellular calcium signaling to parathyroid hormone-related peptide secretion via a Rab11a-dependent and AMSH-sensitive mechanism."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Endocrinol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1210/me.2006-0523"}], "href": "https://doi.org/10.1210/me.2006-0523"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17426287"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17426287"}]}, {"type": "r", "ref": 35, "children": [{"type": "t", "text": "Kenneth L Madsen, Thor S Thorsen, Troels Rahbek-Clemmensen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein interacting with C kinase 1 (PICK1) reduces reinsertion rates of interaction partners sorted to Rab11-dependent slow recycling pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111.294702"}], "href": "https://doi.org/10.1074/jbc.M111.294702"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22303009"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22303009"}]}]}]}