NDLI: Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane

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Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane

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Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gupta, R. S. Khan, I. U. Kammer, G. M. Wallin, R.
Description	Author Affiliation: Khan IU ( Department of Internal Medicine, Wake Forest University School of Medicine, Winston-Salem, N. C. 27157, Canada.);
Abstract	Accumulating evidence suggests that the mitochondrial molecular chaperone heat shock protein 60 (hsp60) also can localize in extramitochondrial sites. However, direct evidence that hsp60 functions as a chaperone outside of mitochondria is presently lacking. A 60-kDa protein that is present in the plasma membrane of a human leukemic CD4(+) CEM-SS T cell line and is phosphorylated by protein kinase A (PKA) was identified as hsp60. An 18-kDa plasma membrane-associated protein coimmunoprecipitated with hsp60 and was identified as histone 2B (H2B). Hsp60 physically associated with H2B when both molecules were in their dephospho forms. By contrast, PKA-catalyzed phosphorylation of both hsp60 and H2B caused dissociation of H2B from hsp60 and loss of H2B from the plasma membrane of intact T cells. These results suggest that (i) hsp60 and H2B can localize in the T cell plasma membrane; (ii) hsp60 functions as a molecular chaperone for H2B; and (iii) PKA-catalyzed phosphorylation of both hsp60 and H2B appears to regulate the attachment of H2B to hsp60. We propose a model in which phosphorylation/dephosphorylation regulates chaperoning of H2B by hsp60 in the plasma membrane.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	18
Volume Number	95
Language	English
Publisher	National Academy of Sciences
Publisher Date	1998-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Chaperonin 60 Metabolism Cyclic AMP-Dependent Protein Kinases Histones Amino Acid Sequence CD4-Positive T-Lymphocytes Catalysis Cell Membrane Mass Spectrometry Microscopy, Confocal Microscopy, Fluorescence Molecular Sequence Data Peptide Mapping Phosphorylation Precipitin Tests Recombinant Proteins Tumor Cells, Cultured Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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