KTN1

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Kinectin 1 (kinesin receptor)
Identifiers
Symbols KTN1 ; CG1; KNT; MU-RMS-40.19
External IDs OMIM600381 MGI109153 HomoloGene135663 GeneCards: KTN1 Gene
RNA expression pattern
PBB GE KTN1 214709 s at tn.png
PBB GE KTN1 200914 x at tn.png
PBB GE KTN1 200915 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3895 16709
Ensembl ENSG00000126777 ENSMUSG00000021843
UniProt Q86UP2 Q61595
RefSeq (mRNA) NM_001079521 NM_008477
RefSeq (protein) NP_001072989 NP_032503
Location (UCSC) Chr 14:
56.03 – 56.17 Mb
Chr 14:
47.66 – 47.74 Mb
PubMed search [1] [2]

Kinectin is a protein that in humans is encoded by the KTN1 gene.[1][2]

Function[edit]

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[edit]

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

References[edit]

  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.  Check date values in: |year= / |date= mismatch (help)
  2. ^ a b "Entrez Gene: KTN1 kinectin 1 (kinesin receptor)". 
  3. ^ Ong LL, Er CP, Ho A, Aung MT, Yu H (Aug 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. 
  4. ^ a b Neudauer CL, Joberty G, Macara IG (Jan 2001). "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10". Biochem. Biophys. Res. Commun. 280 (2): 541–7. doi:10.1006/bbrc.2000.4160. PMID 11162552. 
  5. ^ a b 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. 21 (23): 8022–34. doi:10.1128/MCB.21.23.8022-8034.2001. PMC 99969. PMID 11689693. 
  6. ^ Riento K, Guasch RM, Garg R, Jin B, Ridley AJ (Jun 2003). "RhoE binds to ROCK I and inhibits downstream signaling". Mol. Cell. Biol. 23 (12): 4219–29. doi:10.1128/MCB.23.12.4219-4229.2003. 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. 225 (1): 69–74. doi:10.1006/bbrc.1996.1132. PMID 8769096. 

Further reading[edit]

  • Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S et al. (1994). "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, Tanaka A, Kawarabayasi Y, Sato S et al. (1994). "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, Lemke H, Krönke M (1995). "Molecular cloning and characterization of human kinectin". Mol. Biol. Cell 6 (2): 161–70. doi:10.1091/mbc.6.2.161. PMC 275826. PMID 7787243. 
  • Yu H, Nicchitta CV, Kumar J, Becker M, Toyoshima I, Sheetz MP (1995). "Characterization of kinectin, a kinesin-binding protein: primary sequence and N-terminal topogenic signal analysis". Mol. Biol. Cell 6 (2): 171–83. doi:10.1091/mbc.6.2.171. PMC 275827. PMID 7787244. 
  • Print CG, Leung E, Harrison JE, Watson JD, Krissansen GW (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, Rooke L, Krissansen GW (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. doi:10.1007/s002510050050. PMID 8575822. 
  • Hotta K, Tanaka K, Mino A, Kohno H, Takai Y (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, Koerten HK, Mommaas AM, Van Oostveldt P 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, Lengfelder E, Kellerer AM, Bauchinger M (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, Kuznetsov SA, Yu H (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, Jackson PD, Perry R, Cain 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, Gauthier-Rouvière C, Fort P (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, Hampton B, Burgess WH, Yamada KM (2002). "Integrin clustering induces kinectin accumulation". J. Cell. Sci. 115 (Pt 10): 2031–40. PMID 11973345. 
  • Ong LL, Er CP, Ho A, Aung MT, Yu H (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. 
  • Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K 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.