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Insulin rapidly stimulates ERK2 in the membrane of osteoblast‐like UMR‐106 cell
Author(s) -
Kim SungJin,
Kim KyungHa
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700204841
Subject(s) - osteoblast , microbiology and biotechnology , membrane , insulin , chemistry , cell , endocrinology , medicine , biology , biochemistry , in vitro
We investigated subcellular distribution of ERK2 in osteoblast‐like UMR‐106 cell and explored to determine if its activities are regulated by insulin. 23%, 34% and 43% of total ERK2 were distributed in membrane, cytosol and nucleus, respectively. Insulin caused 40% increase of ERK2 content in membrane in 10 min whereas it induced approximately 50% decrease of ERK2 in cytosol in 10 min. In terms ofkinase activity, insulin stimulated phosphorylation of the membrane‐associated ERK2 by 2‐fold and 1.8‐fold in 1 min and 10 min and cytosolic ERK2 by 2.7‐fold and 2.3‐fold in 1 min and 10 min, respectively. In contrast, the phosphorylation of nuclear ERK2 was stimulated by insulin in time‐dependent manner with maximal (3‐fold) activity observed at 30 min. Insulin also increased the content of MEK2 in membrane by 2.2‐ to 2.6‐fold in 10 min. MEK2 translocated into mambrane in response to insulin may play a role in the activation of the membrane‐associated ERK2 via phosphorylation.