Biology:RAB11A
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Ras-related protein Rab-11A is a protein that in humans is encoded by the RAB11A gene.[1][2]
Function
The protein encoded by this gene belongs to the small GTPase superfamily, Rab family. It is associated with both constitutive and regulated secretory pathways, and may be involved in protein transport.[3]
Rab-11a controls intracellular trafficking of the innate immune receptor TLR4, and thereby also receptor signaling[4]
Interactions
RAB11A has been shown to interact with:
- RAB11FIP1,[5][6][7]
- RAB11FIP2,[8][5][9]
- RAB11FIP3,[5]
- RAB11FIP4,[10] and
- RAB11FIP5[5][9][11]
- Moesin[12]
References
- ↑ "Identification and characterization of a human homolog of the Schizosaccharomyces pombe ras-like gene YPT-3". Oncogene 6 (1): 3–9. January 1991. PMID 1704119.
- ↑ "Human rab11a: transcription, chromosome mapping and effect on the expression levels of host GTP-binding proteins". FEBS Letters 429 (3): 359–64. June 1998. doi:10.1016/S0014-5793(98)00607-3. PMID 9662449.
- ↑ "Entrez Gene: RAB11A RAB11A, member RAS oncogene family". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8766.
- ↑ "The Rab11a GTPase controls Toll-like receptor 4-induced activation of interferon regulatory factor-3 on phagosomes". Immunity 33 (4): 583–96. October 2010. doi:10.1016/j.immuni.2010.09.010. PMID 20933442.
- ↑ 5.0 5.1 5.2 5.3 "Identification and characterization of a family of Rab11-interacting proteins". The Journal of Biological Chemistry 276 (42): 39067–75. October 2001. doi:10.1074/jbc.M104831200. PMID 11495908.
- ↑ "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology 3: 89. 2007. doi:10.1038/msb4100134. PMID 17353931.
- ↑ "Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein". The Journal of Biological Chemistry 277 (14): 12190–9. April 2002. doi:10.1074/jbc.M108665200. PMID 11786538.
- ↑ "Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain". The Journal of Biological Chemistry 277 (30): 27193–9. July 2002. doi:10.1074/jbc.M200757200. PMID 11994279.
- ↑ 9.0 9.1 "Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins". The Journal of Biological Chemistry 276 (42): 38966–70. October 2001. doi:10.1074/jbc.M106133200. PMID 11481332.
- ↑ "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells". Biochemical and Biophysical Research Communications 299 (5): 770–9. December 2002. doi:10.1016/s0006-291x(02)02720-1. PMID 12470645.
- ↑ "A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes". Molecular Cell 6 (6): 1437–48. December 2000. doi:10.1016/s1097-2765(00)00140-4. PMID 11163216.
- ↑ Ramel, Damien; Wang, Xiaobo; Laflamme, Carl; Montell, Denise J.; Emery, Gregory (March 2013). "Rab11 regulates cell–cell communication during collective cell movements" (in en). Nature Cell Biology 15 (3): 317–324. doi:10.1038/ncb2681. ISSN 1465-7392. PMID 23376974.
Further reading
- "Molecular cloning and characterization of a ras p21-like GTP-binding protein (24KG) from rat liver". Biochemical and Biophysical Research Communications 177 (3): 1224–32. June 1991. doi:10.1016/0006-291X(91)90672-T. PMID 1711847.
- "Rab11a is modified in vivo by isoprenoid geranylgeranyl". Electrophoresis 19 (10): 1803–7. July 1998. doi:10.1002/elps.1150191043. PMID 9719562.
- "Identification of a putative effector protein for rab11 that participates in transferrin recycling". Proceedings of the National Academy of Sciences of the United States of America 96 (6): 2840–5. March 1999. doi:10.1073/pnas.96.6.2840. PMID 10077598.
- "Presenilins interact with Rab11, a small GTPase involved in the regulation of vesicular transport". Human Molecular Genetics 8 (7): 1263–9. July 1999. doi:10.1093/hmg/8.7.1263. PMID 10369872.
- "Rab11BP/Rabphilin-11, a downstream target of rab11 small G protein implicated in vesicle recycling". The Journal of Biological Chemistry 274 (36): 25517–24. September 1999. doi:10.1074/jbc.274.36.25517. PMID 10464283.
- "General role of GDP dissociation inhibitor 2 in membrane release of Rab proteins: modulations of its functional interactions by in vitro and in vivo structural modifications". Biochemistry 38 (36): 11711–21. September 1999. doi:10.1021/bi990200r. PMID 10512627.
- "A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes". Molecular Cell 6 (6): 1437–48. December 2000. doi:10.1016/S1097-2765(00)00140-4. PMID 11163216.
- "Myosin vb is associated with plasma membrane recycling systems". Molecular Biology of the Cell 12 (6): 1843–57. June 2001. doi:10.1091/mbc.12.6.1843. PMID 11408590.
- "Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins". The Journal of Biological Chemistry 276 (42): 38966–70. October 2001. doi:10.1074/jbc.M106133200. PMID 11481332.
- "Identification and characterization of a family of Rab11-interacting proteins". The Journal of Biological Chemistry 276 (42): 39067–75. October 2001. doi:10.1074/jbc.M104831200. PMID 11495908.
- "Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein". The Journal of Biological Chemistry 277 (14): 12190–9. April 2002. doi:10.1074/jbc.M108665200. PMID 11786538.
- "Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain". The Journal of Biological Chemistry 277 (30): 27193–9. July 2002. doi:10.1074/jbc.M200757200. PMID 11994279.
- "Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly". The Journal of Biological Chemistry 277 (31): 28271–9. August 2002. doi:10.1074/jbc.M204929200. PMID 12145319.
- "Endogenous plasma membrane t-SNARE syntaxin 4 is present in rab11 positive endosomal membranes and associates with cortical actin cytoskeleton". FEBS Letters 531 (3): 513–9. November 2002. doi:10.1016/S0014-5793(02)03605-0. PMID 12435603.
- "Rab5a and rab11a mediate agonist-induced trafficking of protease-activated receptor 2". American Journal of Physiology. Cell Physiology 284 (5): C1319–29. May 2003. doi:10.1152/ajpcell.00540.2002. PMID 12540381.
- "Mapping of functional domains of gamma-SNAP". The Journal of Biological Chemistry 278 (15): 13531–8. April 2003. doi:10.1074/jbc.M213205200. PMID 12554740.
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