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Two splice variants of CaMKII-anchoring protein are present in the sarcoplasmic reticulum of rabbit fast-twitch muscle.

Abstract：

:Anchoring protein alphaKAP targets calmodulin kinase II (CaMKII) to the sarcoplasmic reticulum (SR), and in the rabbit is a substrate of CaMKII itself in fast-twitch, but not in slow-twitch muscle. This work was aimed at elucidating the molecular basis for differential phosphorylation of alphaKAP. Here we show that two, immunologically related, size forms (23 and 21 kDa) of alphaKAP are present in fast-twitch muscle SR in a 3:1 stoichiometry. Phosphorylation experiments identified the shorter form as the CaMKII specific substrate. Both forms are shown to be stably integrated into the holoenzyme. Two splice variants of alphaKAP were found in rabbit fast-twitch muscle and only one in slow-twitch muscle, using RT-PCR. Mobilities on SDS-PAGE are those expected. The shorter splice variants lacks the 33-nucleotide sequence inserted by alternative splicing present in full-length alphaKAP, akin to differences between variants A and B of brain alphaCaMKII. The absence of the 11-amino acid sequence creates a novel CaMKII phosphorylation site. Taken together our results show that alternative splicing regulates alphaKAP phosphorylation in a fiber-type specific manner.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Damiani E,Sacchetto R,Salviati L,Margreth A

doi

10.1016/s0006-291x(03)00110-4

subject

Has Abstract

pub_date

2003-02-28 00:00:00

pages

73-83

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X03001104

journal_volume

302

pub_type

杂志文章

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