The in vivo phosphorylation sites of bovine αB-crystallin
نویسندگان
چکیده
منابع مشابه
Phosphorylation-induced Change of the Oligomerization State of αB-crystallin*
aB-crystallin in cells can be phosphorylated at three serine residues in response to stress or during mitosis (Ito, H., Okamoto, K., Nakayama, H., Isobe, T., and Kato, K. (1997) J. Biol. Chem. 272, 29934–29941 and Kato, K., Ito, H., Kamei, K., Inaguma, Y., Iwamoto, I., and Saga, S. (1998) J. Biol. Chem. 273, 28346–28354). In the present study, we determined effects of phosphorylation of aBcryst...
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Heath ECROYD*, Sarah MEEHAN*, Joseph HORWITZ†, J. Andrew AQUILINA‡, Justin L. P. BENESCH§, Carol V. ROBINSON§, Cait E. MACPHEE‖ and John A. CARVER*1 *School of Chemistry and Physics, University of Adelaide, Adelaide, SA 5005, Australia, †Jules Stein Institute, University of California, Los Angeles, School of Medicine, Los Angeles, CA 90095-7008, U.S.A., ‡School of Biological Sciences, Universit...
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Relationships between αB-crystallin expression patterns and pathological changes of myocardial cells after heat stress were examined in vitro and in vivo in this study using the H9C2 cell line and Sprague-Dawley rats, respectively. Histopathological lesions, characterized by acute degeneration, karyopyknosis and loss of a defined nucleus, became more severe in rat hearts over the course of heat...
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The β3- and β8-strands and C-terminal residues 155-165 of αB-crystallin were identified by pin arrays as interaction sites for various client proteins including the intermediate filament protein desmin. Here we present data using 5 well-characterised αB-crystallin protein constructs with substituted β3- and β8-strands and with the C-terminal residues 155-165 deleted to demonstrate the importanc...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1989
ISSN: 0014-5793
DOI: 10.1016/0014-5793(89)81491-7