COORDINATION OF 3 SIGNALING ENZYMES BY AKAP79, A MAMMALIAN SCAFFOLD PROTEIN

Citation
Tm. Klauck et al., COORDINATION OF 3 SIGNALING ENZYMES BY AKAP79, A MAMMALIAN SCAFFOLD PROTEIN, Science, 271(5255), 1996, pp. 1589-1592
Citations number
33
Categorie Soggetti
Multidisciplinary Sciences
Journal title
ISSN journal
00368075
Volume
271
Issue
5255
Year of publication
1996
Pages
1589 - 1592
Database
ISI
SICI code
0036-8075(1996)271:5255<1589:CO3SEB>2.0.ZU;2-V
Abstract
Multivalent binding proteins, such as the yeast scaffold protein Steri le-5, coordinate the location of kinases by serving as platforms for t he assembly of signaling units. Similarly, in mammalian cells the cycl ic adenosine 3',5'-monophosphate-dependent protein kinase (PKA) and ph osphatase 2B [calcineurin (CaN)] are complexed by an A kinase anchorin g protein, AKAP79. Deletion analysis and binding studies demonstrate t hat a third enzyme, protein kinase C (PKC), binds AKAP79 at a site dis tinct from those bound by PKA or CaN. The subcellular distributions of PKC and AKAP79 were similar in neurons. Thus, AKAP79 appears to funct ion as a scaffold protein for three multifunctional enzymes.