Biology:TBCD
From HandWiki
Generic protein structure example |
Tubulin-specific chaperone D is a protein that in humans is encoded by the TBCD gene.[1]
Function
Cofactor D is one of four proteins (cofactors A, D, E, and C) involved in the pathway leading to correctly folded beta-tubulin from folding intermediates. Cofactors A and D are believed to play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Cofactor E binds to the cofactor D/beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state.[1]
Interactions
TBCD has been shown to interact with ARL2.[2][3]
References
- ↑ 1.0 1.1 "Entrez Gene: TBCD tubulin folding cofactor D". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6904.
- ↑ "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. October 2003. doi:10.1074/jbc.M308678200. PMID 12912990.
- ↑ "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. May 2000. doi:10.1083/jcb.149.5.1087. PMID 10831612.
Further reading
- "Chaperonin-mediated folding of actin and tubulin". J. Cell Biol. 132 (1–2): 1–4. 1996. doi:10.1083/jcb.132.1.1. PMID 8567715.
- "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. 1996. doi:10.1006/abio.1996.0138. PMID 8619474.
- "Pathway leading to correctly folded beta-tubulin". Cell 86 (2): 287–96. 1996. doi:10.1016/S0092-8674(00)80100-2. PMID 8706133.
- "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. 1997. doi:10.1101/gr.7.4.353. PMID 9110174.
- "Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors". J. Cell Biol. 138 (4): 821–32. 1997. doi:10.1083/jcb.138.4.821. PMID 9265649.
- "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (1): 63–70. 1999. doi:10.1093/dnares/6.1.63. PMID 10231032.
- "Tubulin folding cofactor D is a microtubule destabilizing protein". FEBS Lett. 470 (1): 93–5. 2000. doi:10.1016/S0014-5793(00)01293-X. PMID 10722852.
- "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin". J. Cell Biol. 149 (5): 1087–96. 2000. doi:10.1083/jcb.149.5.1087. PMID 10831612.
- "Shear stress-dependent regulation of the human beta-tubulin folding cofactor D gene". Circ. Res. 87 (12): 1188–94. 2001. doi:10.1161/01.res.87.12.1188. PMID 11110777.
- "Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants". Mol. Vis. 8: 205–20. 2002. PMID 12107410.
- "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". J. Biol. Chem. 278 (42): 40829–36. 2003. doi:10.1074/jbc.M308678200. PMID 12912990.
- "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. 2004. doi:10.1101/gr.2334104. PMID 15231748.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.