MAGNESIUM PROTECTS PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE-MEDIATED INACTIVATION OF CASEIN KINASE-I IN ERYTHROCYTE-MEMBRANE

被引：7

作者：

CHAUHAN, VPS

SINGH, SS

CHAUHAN, A

BROCKERHOFF, H

机构：

[1] NYS Institute for Basic Research in Developmental Disabilities, Staten Island, NY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1177卷 / 03期

关键词：

PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; CASEIN KINASE; PROTEIN PHOSPHORYLATION; MAGNESIUM ION; (ERYTHROCYTE); (RABBIT);

D O I：

10.1016/0167-4889(93)90128-C

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent reports suggest that membrane-bound casein kinase I (MBCK I) activity in erythrocytes is inactivated by exogenously added phosphatidylinositol 4,5-bisphosphate (PIP2) (Bazenet et al. (1990) J. Biol. Chem. 265, 7369-7376; Brockman and Anderson (1991) J. Biol. Chem. 266, 2508-2512). Here we report that PIP2-mediated inhibition of MBCK I in erythrocytes is only observed if exogenous PIP2 and the kinase are allowed to interact in the absence of Mg2+. Prior incubation Of PIP2 with 1 mM Mg2+ prevents the inactivation of MBCK I by PIP2. Other divalent cations (Ni2+, Co2+, Mn2+, Cd2+, Ca2+) and trivalent metal ions (La3+, Cr3+, Al3+) did not protect MBCK I from PIP2-mediated inactivation, indicating that the protective effect is specific for Mg2+ only. We propose a role of Mg2+ in the interaction of CK I with phosphoinositides, and that PIP2-mediated inhibition of protein kinase(s) may be a non-physiological phenomenon.

引用

页码：318 / 321

页数：4

共 18 条

[1]

BAZENET CE, 1990, J BIOL CHEM, V265, P7369

[2]

BERRIDGE MJ, 1987, ANNU REV BIOCHEM, V56, P159, DOI 10.1146/annurev.bi.56.070187.001111

[3] TYROSINE-PROTEIN KINASE INHIBITION IN HUMAN ERYTHROCYTES BY POLYPHOSPHOINOSITIDES (PIP AND PIP2) [J].