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Endoplasmic reticulum stress-inducible protein GRP94 is associated with an Mg2+-dependent serine kinase activity modulated by Ca2+ and GRP78/BiP.
J Cell Physiol. 1997 Feb; 170(2):115-29.JC

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.

Authors+Show Affiliations

Department of Biochemistry and Molecular Biology, University of Southern California School of Medicine, Norris Cancer Center, Los Angeles 90033, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

9009140

Citation

Ramakrishnan, M, et al. "Endoplasmic Reticulum Stress-inducible Protein GRP94 Is Associated With an Mg2+-dependent Serine Kinase Activity Modulated By Ca2+ and GRP78/BiP." Journal of Cellular Physiology, vol. 170, no. 2, 1997, pp. 115-29.
Ramakrishnan M, Schönthal AH, Lee AS. Endoplasmic reticulum stress-inducible protein GRP94 is associated with an Mg2+-dependent serine kinase activity modulated by Ca2+ and GRP78/BiP. J Cell Physiol. 1997;170(2):115-29.
Ramakrishnan, M., Schönthal, A. H., & Lee, A. S. (1997). Endoplasmic reticulum stress-inducible protein GRP94 is associated with an Mg2+-dependent serine kinase activity modulated by Ca2+ and GRP78/BiP. Journal of Cellular Physiology, 170(2), 115-29.
Ramakrishnan M, Schönthal AH, Lee AS. Endoplasmic Reticulum Stress-inducible Protein GRP94 Is Associated With an Mg2+-dependent Serine Kinase Activity Modulated By Ca2+ and GRP78/BiP. J Cell Physiol. 1997;170(2):115-29. PubMed PMID: 9009140.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Endoplasmic reticulum stress-inducible protein GRP94 is associated with an Mg2+-dependent serine kinase activity modulated by Ca2+ and GRP78/BiP. AU - Ramakrishnan,M, AU - Schönthal,A H, AU - Lee,A S, PY - 1997/2/1/pubmed PY - 2000/6/20/medline PY - 1997/2/1/entrez SP - 115 EP - 29 JF - Journal of cellular physiology JO - J Cell Physiol VL - 170 IS - 2 N2 - 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. SN - 0021-9541 UR - https://www.unboundmedicine.com/medline/citation/9009140/Endoplasmic_reticulum_stress_inducible_protein_GRP94_is_associated_with_an_Mg2+_dependent_serine_kinase_activity_modulated_by_Ca2+_and_GRP78/BiP_ L2 - https://doi.org/10.1002/(SICI)1097-4652(199702)170:2<115::AID-JCP3>3.0.CO;2-R DB - PRIME DP - Unbound Medicine ER -