TY - JOUR
T1 - Description of a protein kinase derived from insulin-treated 3T3-L1 cells that catalyzes the phosphorylation of ribosomal protein S6 and casein
AU - Cobb, M. H.
AU - Rosen, O. M.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1983
Y1 - 1983
N2 - Particulate preparations from insulin-treated 3T3-L1 cells retain the enhanced ability to incorporate 32P from [γ-32P]ATP into ribosomal protein S6. A cyclic AMP-independent protein kinase that phosphorylates S6 and casein and that may be involved in the increase in S6 phosphorylation produced by insulin has been isolated based upon the observation that there is 1.5-3.0-fold higher activity in particulate preparations derived from insulin-treated cells than there is in comparable preparations from control cells. The enzyme activity was purified 2071-fold by KCl extraction, phosphocellulose chromatography, and gel filtration. The S6 phosphorylating activity was also characterized by its behavior on casein-Sepharose and DEAE-cellulose chromatography and its sedimentation in glycerol gradients. None of these procedures resolved the S6 and casein kinase activities. Some of the properties of this kinase, including a molecular weight of about 35,000, inhibition of F- or phosphate, chromatography on DEAE-cellulose and phosphocellulose, and insensitivity to inhibition by GTP, are similar to those of a previous described enzyme, casein kinase I.
AB - Particulate preparations from insulin-treated 3T3-L1 cells retain the enhanced ability to incorporate 32P from [γ-32P]ATP into ribosomal protein S6. A cyclic AMP-independent protein kinase that phosphorylates S6 and casein and that may be involved in the increase in S6 phosphorylation produced by insulin has been isolated based upon the observation that there is 1.5-3.0-fold higher activity in particulate preparations derived from insulin-treated cells than there is in comparable preparations from control cells. The enzyme activity was purified 2071-fold by KCl extraction, phosphocellulose chromatography, and gel filtration. The S6 phosphorylating activity was also characterized by its behavior on casein-Sepharose and DEAE-cellulose chromatography and its sedimentation in glycerol gradients. None of these procedures resolved the S6 and casein kinase activities. Some of the properties of this kinase, including a molecular weight of about 35,000, inhibition of F- or phosphate, chromatography on DEAE-cellulose and phosphocellulose, and insensitivity to inhibition by GTP, are similar to those of a previous described enzyme, casein kinase I.
UR - http://www.scopus.com/inward/record.url?scp=0021060888&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021060888&partnerID=8YFLogxK
M3 - Article
C2 - 6313661
AN - SCOPUS:0021060888
SN - 0021-9258
VL - 258
SP - 12472
EP - 12481
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 20
ER -