MAP4

From Wikipedia, the free encyclopedia


Microtubule-associated protein 4
Identifiers
Symbol(s) MAP4; DKFZp779A1753; MGC8617
External IDs OMIM: 157132 MGI97178 HomoloGene1780
Orthologs
Human Mouse
Entrez 4134 17758
Ensembl n/a ENSMUSG00000032479
Uniprot n/a Q05BJ2
Refseq NM_002375 (mRNA)
NP_002366 (protein)
NM_008633 (mRNA)
NP_032659 (protein)
Location n/a Chr 9: 109.82 - 109.93 Mb
Pubmed search [1] [2]

Microtubule-associated protein 4, also known as MAP4, is a human gene.

The protein encoded by this gene is a major non-neuronal microtubule-associated protein. This protein contains a domain similar to the microtubule-binding domains of neuronal microtubule-associated protein (MAP2) and microtubule-associated protein tau (MAPT/TAU). This protein promotes microtubule assembly, and has been shown to counteract destabilization of interphase microtubule catastrophe promotion. Cyclin B was found to interact with this protein, which targets cell division cycle 2 (CDC2) kinase to microtubules. The phosphorylation of this protein affects microtubule properties and cell cycle progression. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed, the full-length nature of three of which are supported.[1]

[edit] References

[edit] Further reading

  • Chapin SJ, Bulinski JC (1993). "Microtubule stabilization by assembly-promoting microtubule-associated proteins: a repeat performance.". Cell Motil. Cytoskeleton 23 (4): 236–43. doi:10.1002/cm.970230403. PMID 1477887. 
  • West RR, Tenbarge KM, Olmsted JB (1991). "A model for microtubule-associated protein 4 structure. Domains defined by comparisons of human, mouse, and bovine sequences.". J. Biol. Chem. 266 (32): 21886–96. PMID 1718985. 
  • Chapin SJ, Bulinski JC (1991). "Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4) contains a domain homologous to the microtubule-binding domains of neuronal MAP2 and tau.". J. Cell. Sci. 98 ( Pt 1): 27–36. PMID 1905296. 
  • Chapin SJ, Lue CM, Yu MT, Bulinski JC (1995). "Differential expression of alternatively spliced forms of MAP4: a repertoire of structurally different microtubule-binding domains.". Biochemistry 34 (7): 2289–301. PMID 7857940. 
  • Ookata K, Hisanaga S, Bulinski JC, et al. (1995). "Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics.". J. Cell Biol. 128 (5): 849–62. PMID 7876309. 
  • Chapin SJ, Bulinski JC (1994). "Cellular microtubules heterogeneous in their content of microtubule-associated protein 4 (MAP4).". Cell Motil. Cytoskeleton 27 (2): 133–49. doi:10.1002/cm.970270205. PMID 7909279. 
  • Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474. 
  • Illenberger S, Drewes G, Trinczek B, et al. (1996). "Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics.". J. Biol. Chem. 271 (18): 10834–43. PMID 8631898. 
  • Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174. 
  • Bulinski JC, McGraw TE, Gruber D, et al. (1998). "Overexpression of MAP4 inhibits organelle motility and trafficking in vivo.". J. Cell. Sci. 110 ( Pt 24): 3055–64. PMID 9365275. 
  • Ookata K, Hisanaga S, Sugita M, et al. (1998). "MAP4 is the in vivo substrate for CDC2 kinase in HeLa cells: identification of an M-phase specific and a cell cycle-independent phosphorylation site in MAP4.". Biochemistry 36 (50): 15873–83. doi:10.1021/bi971251w. PMID 9398320. 
  • Nguyen HL, Gruber D, Bulinski JC (1999). "Microtubule-associated protein 4 (MAP4) regulates assembly, protomer-polymer partitioning and synthesis of tubulin in cultured cells.". J. Cell. Sci. 112 ( Pt 12): 1813–24. PMID 10341201. 
  • Ebneth A, Drewes G, Mandelkow EM, Mandelkow E (2000). "Phosphorylation of MAP2c and MAP4 by MARK kinases leads to the destabilization of microtubules in cells.". Cell Motil. Cytoskeleton 44 (3): 209–24. doi:10.1002/(SICI)1097-0169(199911)44:3<209::AID-CM6>3.0.CO;2-4. PMID 10542369. 
  • Kitazawa H, Iida J, Uchida A, et al. (2000). "Ser787 in the proline-rich region of human MAP4 is a critical phosphorylation site that reduces its activity to promote tubulin polymerization.". Cell Struct. Funct. 25 (1): 33–9. PMID 10791892. 
  • Chang W, Gruber D, Chari S, et al. (2002). "Phosphorylation of MAP4 affects microtubule properties and cell cycle progression.". J. Cell. Sci. 114 (Pt 15): 2879–87. PMID 11683421. 
  • Iida J, Itoh TJ, Hotani H, et al. (2002). "The projection domain of MAP4 suppresses the microtubule-bundling activity of the microtubule-binding domain.". J. Mol. Biol. 320 (1): 97–106. doi:10.1016/S0022-2836(02)00402-3. PMID 12079337. 
  • Holmfeldt P, Brattsand G, Gullberg M (2002). "MAP4 counteracts microtubule catastrophe promotion but not tubulin-sequestering activity in intact cells.". Curr. Biol. 12 (12): 1034–9. PMID 12123579. 
  • 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. PMID 12477932. 
  • Tokuraku K, Matsushima K, Matui T, et al. (2003). "The number of repeat sequences in microtubule-associated protein 4 affects the microtubule surface properties.". J. Biol. Chem. 278 (32): 29609–18. doi:10.1074/jbc.M302186200. PMID 12773533.