KTN1

From Wikipedia, the free encyclopedia
Kinectin 1 (kinesin receptor)
Identifiers
SymbolsKTN1; CG1; KNT; MU-RMS-40.19
External IDsOMIM: 600381 MGI: 109153 HomoloGene: 7397 GeneCards: KTN1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez389516709
EnsemblENSG00000126777ENSMUSG00000021843
UniProtQ86UP2Q61595
RefSeq (mRNA)NM_001079521NM_008477
RefSeq (protein)NP_001072989NP_032503
Location (UCSC)Chr 14:
56.03 – 56.17 Mb		Chr 14:
47.66 – 47.74 Mb
PubMed search
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Kinectin is a protein that in humans is encoded by the KTN1 gene.[1][2]

Various cellular organelles and vesicles are transported along the microtubules in the cytoplasm. Likewise, membrane recycling of the endoplasmic reticulum (ER), Golgi assembly at the microtubule organizing center, and alignment of lysosomes along microtubules are all related processes. The transport of organelles requires a special class of microtubule-associated proteins (MAPs). One of these is the molecular motor kinesin (see MIM 148760 and MIM 600025), an ATPase that moves vesicles unidirectionally toward the plus end of the microtubule. Another such MAP is kinectin, a large integral ER membrane protein. Antibodies directed against kinectin have been shown to inhibit its binding to kinesin.[supplied by OMIM][2]

Interactions

KTN1 has been shown to interact with EEF1D,[3] RhoG[4][5] and RHOA.[4][5][6][7]

References

  1. ↑ Rao PN, Yu H, Hodge R, Pettenati MJ, Sheetz MP (Jun 1998). "Assignment of the human kinectin gene (KTN1), encoding a kinesin-binding protein, to chromosome 14 band q22.1 by in situ hybridization". Cytogenet Cell Genet 79 (3–4): 196–7. doi:10.1159/000134719. PMID 9605849. 
  2. ↑ 2.0 2.1 "Entrez Gene: KTN1 kinectin 1 (kinesin receptor)". 
  3. ↑ Ong, Lee-Lee; Er Connie P N, Ho Andrea, Aung May T, Yu Hanry (Aug 2003). "Kinectin anchors the translation elongation factor-1 delta to the endoplasmic reticulum". J. Biol. Chem. (United States) 278 (34): 32115–23. doi:10.1074/jbc.M210917200. ISSN 0021-9258. PMID 12773547. 
  4. ↑ 4.0 4.1 Neudauer, C L; Joberty G, Macara I G (Jan 2001). "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10". Biochem. Biophys. Res. Commun. (United States) 280 (2): 541–7. doi:10.1006/bbrc.2000.4160. ISSN 0006-291X. PMID 11162552. 
  5. ↑ 5.0 5.1 Vignal, E; Blangy A, Martin M, Gauthier-Rouvière C, Fort P (Dec 2001). "Kinectin Is a Key Effector of RhoG Microtubule-Dependent Cellular Activity". Mol. Cell. Biol. (United States) 21 (23): 8022–34. doi:10.1128/MCB.21.23.8022-8034.2001. ISSN 0270-7306. PMC 99969. PMID 11689693. 
  6. ↑ Riento, Kirsi; Guasch Rosa M, Garg Ritu, Jin Boquan, Ridley Anne J (Jun 2003). "RhoE Binds to ROCK I and Inhibits Downstream Signaling". Mol. Cell. Biol. (United States) 23 (12): 4219–29. doi:10.1128/MCB.23.12.4219-4229.2003. ISSN 0270-7306. PMC 156133. PMID 12773565. 
  7. ↑ Hotta, K; Tanaka K, Mino A, Kohno H, Takai Y (Aug 1996). "Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor". Biochem. Biophys. Res. Commun. (UNITED STATES) 225 (1): 69–74. doi:10.1006/bbrc.1996.1132. ISSN 0006-291X. PMID 8769096. 

Further reading

  • Nomura N, Miyajima N, Sazuka T, et al. (1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1". DNA Res. 1 (1): 27–35. doi:10.1093/dnares/1.1.27. PMID 7584026. 
  • Nomura N, Miyajima N, Sazuka T, et al. (1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement)". DNA Res. 1 (1): 47–56. doi:10.1093/dnares/1.1.47. PMID 7584028. 
  • Fütterer A, Kruppa G, Krämer B, et al. (1995). "Molecular cloning and characterization of human kinectin". Mol. Biol. Cell 6 (2): 161–70. PMC 275826. PMID 7787243. 
  • Yu H, Nicchitta CV, Kumar J, et al. (1995). "Characterization of kinectin, a kinesin-binding protein: primary sequence and N-terminal topogenic signal analysis". Mol. Biol. Cell 6 (2): 171–83. PMC 275827. PMID 7787244. 
  • Print CG, Leung E, Harrison JE, et al. (1994). "Cloning of a gene encoding a human leukocyte protein characterised by extensive heptad repeats". Gene 144 (2): 221–8. doi:10.1016/0378-1119(94)90381-6. PMID 8039706. 
  • Print CG, Morris CM, Spurr NK, et al. (1996). "The CG-1 gene, a member of the kinectin and ES/130 family, maps to human chromosome band 14q22". Immunogenetics 43 (4): 227–9. PMID 8575822. 
  • Hotta K, Tanaka K, Mino A, et al. (1996). "Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor". Biochem. Biophys. Res. Commun. 225 (1): 69–74. doi:10.1006/bbrc.1996.1132. PMID 8769096. 
  • Alberts AS, Bouquin N, Johnston LH, Treisman R (1998). "Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7". J. Biol. Chem. 273 (15): 8616–22. doi:10.1074/jbc.273.15.8616. PMID 9535835. 
  • Vancoillie G, Lambert J, Mulder A, et al. (2000). "Kinesin and kinectin can associate with the melanosomal surface and form a link with microtubules in normal human melanocytes". J. Invest. Dermatol. 114 (3): 421–9. doi:10.1046/j.1523-1747.2000.00896.x. PMID 10692099. 
  • Salassidis K, Bruch J, Zitzelsberger H, et al. (2000). "Translocation t(10;14)(q11.2:q22.1) fusing the kinetin to the RET gene creates a novel rearranged form (PTC8) of the RET proto-oncogene in radiation-induced childhood papillary thyroid carcinoma". Cancer Res. 60 (11): 2786–9. PMID 10850414. 
  • Ong LL, Lim AP, Er CP, et al. (2000). "Kinectin-kinesin binding domains and their effects on organelle motility". J. Biol. Chem. 275 (42): 32854–60. doi:10.1074/jbc.M005650200. PMID 10913441. 
  • Harrington JJ, Sherf B, Rundlett S, et al. (2001). "Creation of genome-wide protein expression libraries using random activation of gene expression". Nat. Biotechnol. 19 (5): 440–5. doi:10.1038/88107. PMID 11329013. 
  • Vignal E, Blangy A, Martin M, et al. (2001). "Kinectin Is a Key Effector of RhoG Microtubule-Dependent Cellular Activity". Mol. Cell. Biol. 21 (23): 8022–34. doi:10.1128/MCB.21.23.8022-8034.2001. PMC 99969. PMID 11689693. 
  • Tran H, Pankov R, Tran SD, et al. (2003). "Integrin clustering induces kinectin accumulation". J. Cell. Sci. 115 (Pt 10): 2031–40. PMID 11973345. 
  • 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. 
  • Heilig R, Eckenberg R, Petit JL, et al. (2003). "The DNA sequence and analysis of human chromosome 14". Nature 421 (6923): 601–7. doi:10.1038/nature01348. PMID 12508121. 
  • Ong LL, Er CP, Ho A, et al. (2003). "Kinectin anchors the translation elongation factor-1 delta to the endoplasmic reticulum". J. Biol. Chem. 278 (34): 32115–23. doi:10.1074/jbc.M210917200. PMID 12773547. 
  • 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. 
  • Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. 


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