MISC

2000年2月

Ser787 in the proline-rich region of human MAP4 is a critical phosphorylation site that reduces its activity to promote tubulin polymerization

CELL STRUCTURE AND FUNCTION
  • H Kitazawa
  • ,
  • J Iida
  • ,
  • A Uchida
  • ,
  • K Haino-Fukushima
  • ,
  • TJ Itoh
  • ,
  • H Hotani
  • ,
  • K Ookata
  • ,
  • H Murofushi
  • ,
  • JC Bulinski
  • ,
  • T Kishimoto
  • ,
  • S Hisanaga

25
1
開始ページ
33
終了ページ
39
記述言語
英語
掲載種別
DOI
10.1247/csf.25.33
出版者・発行元
JAPAN SOC CELL BIOLOGY

p34(cdc2) kinase-phosphorylation sires in the microtubule (MT)-binding region of MAP4 were determined by peptide sequence of phosphorylated MTB3, a fragment containing the carboxy-terminal half of human MAP4. In addition to two phosphopeptides containing Ser696 and Ser787 which were previously indicated to be in vivo phosphorylation sites, two novel phosphopeptides, containing Thr892 or Thr901 and Thr917 as possible phosphorylation sites, were isolated, though only in in vitro phosphorylation. The role of phosphorylation at Ser696 and Ser787, which were differently phosphorylated during the cell cycle (Ookata et al., (1997), Biochemistry: 36: 15873-15883), was investigated in MT-polymerization, using MAP4 Ser to Glu mutants, which mimic phosphorylation at each site. Mutation of Ser787 to Glu strikingly reduced the MAP4's MT-polymerization activity, while Glu-mutation at Ser696 did not. These results suggest that Ser787 could be the critical phosphorylation site causing MTs to be dynamic at mitosis.

Web of Science ® 被引用回数 : 26

リンク情報
DOI
https://doi.org/10.1247/csf.25.33
CiNii Articles
http://ci.nii.ac.jp/naid/10006678784
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/10791892
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000086482800004&DestApp=WOS_CPL

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