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Plant calreticulin is specifically and efficiently phosphorylated by protein kinase CK2.

Abstract：

:Calreticulin isolated from spinach leaves has been specifically phosphorylated in vitro by protein kinase CK2 while animal calreticulin from rabbit liver is not a substrate of this kinase under the same conditions. Phosphoserine is the only phosphoamino acid detected. High affinity binding (Km = 4.4 microM) and a nearly stoichiometric incorporation of phosphate was determined. Partially purified spinach calreticulin is phosphorylated at the same site(s) by a copurifying protein kinase sharing biochemical properties very similar if not identical to those of mammalian CK2. Other plant calreticulins isolated from Liriodendron tulipifera appear to be also phosphorylated by CK2.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Baldan B,Navazio L,Friso A,Mariani P,Meggio F

doi

10.1006/bbrc.1996.0625

subject

Has Abstract

pub_date

1996-04-25 00:00:00

pages

498-502

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)90625-7

journal_volume

221

pub_type

杂志文章

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