{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTIMM29 (also known as Tim29 or C19orf52) is a metazoan‐specific subunit of the human TIM22 complex, which mediates the import of hydrophobic, multi‐transmembrane proteins into the mitochondrial inner membrane. Integrated into the inner membrane with its C‑terminus exposed to the intermembrane space, TIMM29 is essential for complex stability and the proper assembly of hTim22, while also establishing contacts with the translocase of the outer mitochondrial membrane (TOM complex) to facilitate the transfer of hydrophobic carriers across the aqueous intermembrane space."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdvanced crosslinking mass spectrometry studies of the human TIM22 complex support a defined molecular arrangement of its subunits, including TIMM29. This data reinforces its role as an integral structural member of the 440 kDa assembly, further supporting its involvement in maintaining the architecture and functional dynamics of the mitochondrial carrier translocase."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its canonical function in mitochondrial protein import, TIMM29 has been implicated in modulating hepatitis B virus (HBV) amplification. It interacts with the preS1 region of the HBV large S protein, with overexpression of TIMM29 leading to a significant reduction in viral antigens and HBV DNA levels, likely through the modulation of host transcriptional regulators such as SRSF1. Conversely, knockout of TIMM29 results in enhanced HBV replication, highlighting a dual role for TIMM29 in both mitochondrial integrity and host antiviral defense."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Yilin Kang, Michael James Baker, Michael Liem, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tim29 is a novel subunit of the human TIM22 translocase and is involved in complex assembly and stability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Elife (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.7554/eLife.17463"}], "href": "https://doi.org/10.7554/eLife.17463"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27554484"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27554484"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Sylvie Callegari, Frank Richter, Katarzyna Chojnacka, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TIM29 is a subunit of the human carrier translocase required for protein transport."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/1873-3468.12450"}], "href": "https://doi.org/10.1002/1873-3468.12450"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27718247"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27718247"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Anusha Valpadashi, Sylvie Callegari, Andreas Linden, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Defining the architecture of the human TIM22 complex by chemical crosslinking."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/1873-3468.13978"}], "href": "https://doi.org/10.1002/1873-3468.13978"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33125709"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33125709"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Nelly Gakii Muriungi, Keiji Ueda "}, {"type": "b", "children": [{"type": "t", "text": "TIMM29 interacts with hepatitis B virus preS1 to modulate the HBV life cycle."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Microbiol Immunol (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/1348-0421.12852"}], "href": "https://doi.org/10.1111/1348-0421.12852"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32970362"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32970362"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Lin Guo, Jia-Jun Liu, Shao-Yuan Long, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TIM22 and TIM29 inhibit HBV replication by up-regulating SRSF1 expression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Med Virol (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jmv.29439"}], "href": "https://doi.org/10.1002/jmv.29439"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38294104"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38294104"}]}]}]}