Abstract:
:The 94-kDa glucose-regulated protein (GRP94) is a glycoprotein in the endoplasmic reticulum (ER). It has been characterized as a Ca2+-binding protein and a molecular chaperone. In this report we show that highly purified GRP94 exhibits an active Mg2+-dependent serine kinase activity (termed 94-kinase). The 94-kinase can be recovered from ER membrane fractions and is able to phosphorylate both the constitutive and stress-induced forms of GRP94, correlating with their induction kinetics. The 94-kinase activity is distinct from casein kinase II. In contrast to the heat-stable, Ca2+-dependent autophosphorylation activity recently reported for GRP94, the labile 94-kinase activity is inhibited by Ca2+. We determined that the phosphopeptide map of in vitro phosphorylated GRP94 by the 94-kinase resembles that of the in vivo phosphorylated GRP94. Further, the 94-kinase activity can be specifically stimulated by GRP78, a coregulated protein in the ER known to interact with GRP94.
journal_name
J Cell Physioljournal_title
Journal of cellular physiologyauthors
Ramakrishnan M,Schönthal AH,Lee ASdoi
10.1002/(SICI)1097-4652(199702)170:2<115::AID-JCP3subject
Has Abstractpub_date
1997-02-01 00:00:00pages
115-29issue
2eissn
0021-9541issn
1097-4652pii
10.1002/(SICI)1097-4652(199702)170:2<115::AID-JCP3journal_volume
170pub_type
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