✦ LIBER ✦

Calpain-mediated proteolysis of microtubule-associated protein 2 (MAP-2) is inhibited by phosphorylation by cAMP-dependent protein kinase, but not by Ca2+/calmodulin-dependent protein kinase II

✍ Scribed by Dr. Gail V. W. Johnson; V. G. Foley

Publisher: John Wiley and Sons
Year: 1993
Tongue: English
Weight: 686 KB
Volume: 34
Category: Article
ISSN: 0360-4012
DOI: 10.1002/jnr.490340607

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✦ Synopsis

B i k n g h a m , Alabama -

The effects of CAMP-dependent protein kinase (CAMP-PK) and CaZf/calmodulin-dependent protein kinase I1 (CaMKII) phosphorylation on the calpainmediated degradation of microtubule-associated protein 2 (MAP-2) were studied. Both CAMP-PK and CaMKII readily phosphorylated MAP-2. However, CAMP-PK phosphorylated MAP-2 to a significantly greater extent than did CaMKII (4.5 mol 32P/mol MAP-2 and 1.4 mol "P/mol MAP-2, respectively). Phosphorylation of MAP-2 by CAMP-PK, but not by CaMKII, significantly inhibited the calpain-induced hydrolysis of MAP-2. These results demonstrate that the phosphorylation of sites on the MAP-2 molecule accessible to CAMP-PK, but not to CaMKII, result in increased resistance to calpain proteolysis.

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