{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMYO5A, which encodes the actin‐based motor protein myosin Va, plays a central role in the intracellular transport of pigment‐containing organelles in melanocytes. In this context, myosin Va interacts with Rab27a and its effectors such as melanophilin to link melanosomes to the cortical actin network, thereby regulating their peripheral distribution and normal pigmentation. Disruption of these interactions, as seen in Griscelli syndrome patients and relevant animal models, leads to pigment dilution and neurological deficits. Detailed studies using isoform‐specific knockdown have further shown that alternative splicing (e.g., inclusion of exon F) directs myosin Va to melanosomes, ensuring their proper transit in melanocytes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond pigmentation, myosin Va is integral to the targeted delivery of secretory vesicles and the recycling of membrane proteins in diverse cell types. In pancreatic β‐cells, neuroendocrine cells, and neurons, myosin Va couples with distinct Rab GTPases (including Rab3A, Rab10, Rab11, and others) to recruit or dock vesicles at the plasma membrane, thereby ensuring efficient exocytosis of insulin and neurotransmitters. Moreover, myosin Va is implicated in specialized processes such as ciliogenesis by mediating the transport of preciliary vesicles to the centrosome and by interacting with centrosome‐associated proteins. Its function has also been extended to the egress of viral particles in infected cells, to the regulation of endothelial secretion of von Willebrand factor, and even to mucin release in airway epithelia."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nStructural and mechanistic studies have elucidated the molecular basis for myosin Va’s diverse functions. Its extended globular tail domain contains multiple Rab‐binding sites that, through alternative splicing and regulated dimerization, govern autoinhibition and cargo specificity. Calmodulin binding to defined IQ motifs modulates its motor activity in response to Ca²⁺ signals, while kinetic and simulation studies have detailed its hand‐over‐hand stepping during cargo transport along actin filaments. In addition, aberrant expression, gene fusions, or mutation of MYO5A have been linked to enhanced cancer cell migration and metastasis as well as to defects in mRNA transport and processing, highlighting its multifaceted regulatory roles in cell physiology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Molly Strom, Alistair N Hume, Abul K Tarafder, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M202574200"}], "href": "https://doi.org/10.1074/jbc.M202574200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11980908"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11980908"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Gaël Ménasché, Chen Hsuan Ho, Ozden Sanal, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Griscelli syndrome restricted to hypopigmentation results from a melanophilin defect (GS3) or a MYO5A F-exon deletion (GS1)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI18264"}], "href": "https://doi.org/10.1172/JCI18264"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12897212"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12897212"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Ozden Sanal, Fúgen Ersoy, Ilhan Tezcan, et al. 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