Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
KIFAP3
Introduction
Kinesin-associated protein 3 is a protein that in humans is encoded by the KIFAP3 (also known as KAP3) gene.[1][2] It is a non-motor, accessory subunit which co-oligomerizes with the motor subunits KIF3A and KIF3B or KIF3C, to form heterotrimeric kinesin-2 motor proteins. Kinesin-2 KAP subunits were initially characterized in echinoderms and mice.[3][4]
Function
Function
The small G protein GDP dissociation stimulator (smg GDS) is a regulator protein having two activities on a group of small G proteins including the Rho and Rap1 family members and Ki-Ras; one is to stimulate their GDP/GTP exchange reactions, and the other is to inhibit their interactions with membranes. The protein encoded by this gene contains 9 Armadillo repeats and interacts with the smg GDS protein through these repeats. This protein, which is highly concentrated around the endoplasmic reticulum, is phosphorylated by v-src , and this phosphorylation reduces the affinity of the protein for smg GDS. It is thought that this protein serves as a linker between human chromosome-associated polypeptide (HCAP) and KIF3A/B, a kinesin superfamily protein in the nucleus, and that it plays a role in the interaction of chromosomes with an ATPase motor protein.[2]
References
References
- ↑ 1.0 1.1 Shimizu K, Kawabe H, Minami S, Honda T, Takaishi K, Shirataki H, Takai Y (Dec 1996). “SMAP, an Smg GDS-associating protein having arm repeats and phosphorylated by Src tyrosine kinase”. J Biol Chem. 271 (43): 27013–7. doi:10.1074/jbc.271.43.27013. PMID 8900189.
- ↑ 2.0 2.1 “Entrez Gene: KIFAP3 kinesin-associated protein 3”.
- ↑ Wedaman KP, Meyer DW, Rashid DJ, Cole DG, Scholey JM (February 1996). “Sequence and submolecular localization of the 115-kD accessory subunit of the heterotrimeric kinesin-II (KRP85/95) complex”. J. Cell Biol. 132 (3): 371–80. doi:10.1083/jcb.132.3.371. PMC 2120715. PMID 8636215.
- ↑ Yamazaki H, Nakata T, Okada Y, Hirokawa N (August 1996). “Cloning and characterization of KAP3: a novel kinesin superfamily-associated protein of KIF3A/3B”. Proc. Natl. Acad. Sci. U.S.A. 93 (16): 8443–8. doi:10.1073/pnas.93.16.8443. PMC 38690. PMID 8710890.
- ↑ Jimbo T, Kawasaki Y, Koyama R, Sato R, Takada S, Haraguchi K, Akiyama T (April 2002). “Identification of a link between the tumour suppressor APC and the kinesin superfamily”. Nat. Cell Biol. 4 (4): 323–7. doi:10.1038/ncb779. PMID 11912492.
- ↑ Shimizu K, Shirataki H, Honda T, Minami S, Takai Y (March 1998). “Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide”. J. Biol. Chem. 273 (12): 6591–4. doi:10.1074/jbc.273.12.6591. PMID 9506951.
Further reading
Further reading
- Nagata K, Puls A, Futter C, et al. (1998). “The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3”. EMBO J. 17 (1): 149–58. doi:10.1093/emboj/17.1.149. PMC 1170366. PMID 9427749.
- Shimizu K, Shirataki H, Honda T, et al. (1998). “Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide”. J. Biol. Chem. 273 (12): 6591–4. doi:10.1074/jbc.273.12.6591. PMID 9506951.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Khanna H, Hurd TW, Lillo C, et al. (2005). “RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with SMC1, SMC3, and microtubule transport proteins”. J. Biol. Chem. 280 (39): 33580–7. doi:10.1074/jbc.M505827200. PMC 1249479. PMID 16043481.
- Rual JF, Venkatesan K, Hao T, et al. (2005). “Towards a proteome-scale map of the human protein-protein interaction network”. Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Brown CL, Maier KC, Stauber T, et al. (2006). “Kinesin-2 is a motor for late endosomes and lysosomes”. Traffic. 6 (12): 1114–24. doi:10.1111/j.1600-0854.2005.00347.x. PMID 16262723.
- Haraguchi K, Hayashi T, Jimbo T, et al. (2006). “Role of the kinesin-2 family protein, KIF3, during mitosis”. J. Biol. Chem. 281 (7): 4094–9. doi:10.1074/jbc.M507028200. PMID 16298999.
- Gregory SG, Barlow KF, McLay KE, et al. (2006). “The DNA sequence and biological annotation of human chromosome 1”. Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
- Lim J, Hao T, Shaw C, et al. (2006). “A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration”. Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
- Kuraguchi M, Wang XP, Bronson RT, et al. (2006). “Adenomatous Polyposis Coli (APC) Is Required for Normal Development of Skin and Thymus”. PLoS Genet. 2 (9): e146. doi:10.1371/journal.pgen.0020146. PMCÂ 1564426. PMIDÂ 17002498.
- Stauber T, Simpson JC, Pepperkok R, Vernos I (2007). “A role for kinesin-2 in COPI-dependent recycling between the ER and the Golgi complex”. Curr. Biol. 16 (22): 2245–51. doi:10.1016/j.cub.2006.09.060. PMID 17113389.