Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain

被引:72
作者
Trendelenburg, G [1 ]
Hummel, M [1 ]
Riecken, EO [1 ]
Hanski, C [1 ]
机构
[1] FREE UNIV BERLIN,KLINIKUM BENJAMIN FRANKLIN,DEPT PATHOL,D-12200 BERLIN,GERMANY
关键词
D O I
10.1006/bbrc.1996.1172
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
The cytosolic cAMP activates in eukaryotic cells several isoforms of cAMP-dependent protein kinase (PKAs) involved in signal transduction. The effects of individual PKA isoforms are determined by their cellular localisation, specified through binding to distinct A Kinase Anchor Proteins (AKAPs). A new member of the AKAP family, a membrane-anchored 903 amino acid long protein, designated AKAP149, is characterized in the present work. It is a putative splicing variant of S-AKAP84 with the important new feature of a RNA-binding motif (KH domain). This domain together with the known characteristics of AKAPs suggests the involvement of AKAP149 in the phosphorylation-dependent regulation of RNA-processing. (C) 1996 Academic Press, Inc.
引用
收藏
页码:313 / 319
页数:7
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