| Literature DB >> 8769136 |
G Trendelenburg1, M Hummel, E O Riecken, C Hanski.
Abstract
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.Entities:
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Year: 1996 PMID: 8769136 DOI: 10.1006/bbrc.1996.1172
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575