The unique N-terminal domain of the cAMP phosphodiesterase PDE4D4 allows for interaction with specific SH3 domains

被引：52
作者：
Beard, MB
O'Connell, JC
Bolger, GB
Houslay, MD
机构：
[1] Univ Glasgow, Div Biochem & Mol Biol, Mol Pharmacol Grp, IBLS, Glasgow G12 8QQ, Lanark, Scotland
[2] Univ Utah, Vet Affairs Med Ctr, Dept Med Dvn Oncol, Salt Lake City, UT 84148 USA
[3] Univ Utah, Vet Affairs Med Ctr, Dept Oncol Sci, Salt Lake City, UT 84148 USA
来源：
FEBS LETTERS | 1999年 / 460卷 / 01期
基金：
英国惠康基金;
关键词：
cAMP phosphodiesterase; src homology 3 domain; src family tyrosyl kinase; lyn; protein-protein interaction; compartmentalisation;
D O I：
10.1016/S0014-5793(99)01335-6
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Of the five PDE4D isoenzymes, only the PDE4D4 cAMP specific phosphodiesterase mas able to bind to SH3 domains. Only PDE4D4 and PDE4A5, but not any other PDE4A, B, C and D isoforms expressed in rat brain, bound to src, lyn and fyn kinase SH3 domains, Purified PDE4D4 could bind to purified lyn SH3. PDE4D4 and PDE4A5 both exhibited selectivity for binding the SH3 domains of certain proteins. PDE4D4 did not bind to WW domains. We suggest that an important function of the unique N-terminal region of PDE4D4 may be to allow for association with certain SH3 domain-containing proteins, (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码：173 / 177
页数：5
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