Protein kinase Cδ participates in insulin-induced activation of PKB via PDK1

Chagit Brand; Michal Cipok; Veronique Attali; Asia Bak; Sanford R. Sampson

doi:10.1016/j.bbrc.2006.08.100

Protein kinase Cδ participates in insulin-induced activation of PKB via PDK1

Chagit Brand, Michal Cipok, Veronique Attali, Asia Bak, Sanford R. Sampson

The Mina and Everard Goodman Faculty of Life Sciences

Bar-Ilan University

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

Abstract

PKCδ has been shown to be activated by insulin and to interact with insulin receptor and IRS. PKB(Akt) plays an important role in glucose transport and glycogen synthesis. In this study, we investigated the possibility that PKCδ may be involved in insulin-induced activation of PKB. Studies were conducted on primary cultures of rat skeletal muscle. PKB was activated by insulin stimulation within 5 min and reached a peak by 15-30 min. Insulin also increased the physical association between PKCδ with PKB and with PDK1. The insulin-induced PKCδ-PKB association was PI3K dependent. PKB-PKCδ association was accounted for by the involvement of PDK1. Overexpression of dominant negative PKCδ abrogated insulin-induced association of PKCδ with both PKB and PDK1. Blockade of PKCδ also decreased insulin-induced Thr308 PKB phosphorylation and PKB translocation. Moreover, PKCδ inhibition reduced insulin-induced GSK3 phosphorylation. The results indicate that insulin-activated PKCδ interacts with PDK1 to regulate PKB.

Original language	English
Pages (from-to)	954-962
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	349
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2006.08.100
State	Published - 27 Oct 2006

Bibliographical note

Funding Information:
Supported in part by the Russell Berrie Foundation and D-Cure, Diabetes Care in Israel, the Sorrell Foundation, and grants from The Israel Science Foundation founded by the Israel Academy of Sciences and Humanities, and from the Chief Scientist’s Office of the Israel Ministry of Health. SRS is the incumbent of the Louis Fisher Chair in Cellular Pathology.

Funding

Supported in part by the Russell Berrie Foundation and D-Cure, Diabetes Care in Israel, the Sorrell Foundation, and grants from The Israel Science Foundation founded by the Israel Academy of Sciences and Humanities, and from the Chief Scientist’s Office of the Israel Ministry of Health. SRS is the incumbent of the Louis Fisher Chair in Cellular Pathology.

Funders	Funder number
Diabetes Care in Israel
Russell Berrie Foundation
Sorrell Foundation
Israel Academy of Sciences and Humanities
Israel Science Foundation
Office of the Chief Scientist, Ministry of Health

Keywords

Glucose uptake
Glycogenesis
Insulin
Insulin signaling
PDK1
Protein kinase B
Protein kinase Cδ
Skeletal muscle

Access to Document

10.1016/j.bbrc.2006.08.100

Cite this

@article{d479b0f6b4374739bf845e5d3b6a6238,

title = "Protein kinase Cδ participates in insulin-induced activation of PKB via PDK1",

abstract = "PKCδ has been shown to be activated by insulin and to interact with insulin receptor and IRS. PKB(Akt) plays an important role in glucose transport and glycogen synthesis. In this study, we investigated the possibility that PKCδ may be involved in insulin-induced activation of PKB. Studies were conducted on primary cultures of rat skeletal muscle. PKB was activated by insulin stimulation within 5 min and reached a peak by 15-30 min. Insulin also increased the physical association between PKCδ with PKB and with PDK1. The insulin-induced PKCδ-PKB association was PI3K dependent. PKB-PKCδ association was accounted for by the involvement of PDK1. Overexpression of dominant negative PKCδ abrogated insulin-induced association of PKCδ with both PKB and PDK1. Blockade of PKCδ also decreased insulin-induced Thr308 PKB phosphorylation and PKB translocation. Moreover, PKCδ inhibition reduced insulin-induced GSK3 phosphorylation. The results indicate that insulin-activated PKCδ interacts with PDK1 to regulate PKB.",

keywords = "Glucose uptake, Glycogenesis, Insulin, Insulin signaling, PDK1, Protein kinase B, Protein kinase Cδ, Skeletal muscle",

author = "Chagit Brand and Michal Cipok and Veronique Attali and Asia Bak and Sampson, {Sanford R.}",

note = "Funding Information: Supported in part by the Russell Berrie Foundation and D-Cure, Diabetes Care in Israel, the Sorrell Foundation, and grants from The Israel Science Foundation founded by the Israel Academy of Sciences and Humanities, and from the Chief Scientist{\textquoteright}s Office of the Israel Ministry of Health. SRS is the incumbent of the Louis Fisher Chair in Cellular Pathology.",

year = "2006",

month = oct,

day = "27",

doi = "10.1016/j.bbrc.2006.08.100",

language = "אנגלית",

volume = "349",

pages = "954--962",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Protein kinase Cδ participates in insulin-induced activation of PKB via PDK1

AU - Brand, Chagit

AU - Cipok, Michal

AU - Attali, Veronique

AU - Bak, Asia

AU - Sampson, Sanford R.

N1 - Funding Information: Supported in part by the Russell Berrie Foundation and D-Cure, Diabetes Care in Israel, the Sorrell Foundation, and grants from The Israel Science Foundation founded by the Israel Academy of Sciences and Humanities, and from the Chief Scientist’s Office of the Israel Ministry of Health. SRS is the incumbent of the Louis Fisher Chair in Cellular Pathology.

PY - 2006/10/27

Y1 - 2006/10/27

N2 - PKCδ has been shown to be activated by insulin and to interact with insulin receptor and IRS. PKB(Akt) plays an important role in glucose transport and glycogen synthesis. In this study, we investigated the possibility that PKCδ may be involved in insulin-induced activation of PKB. Studies were conducted on primary cultures of rat skeletal muscle. PKB was activated by insulin stimulation within 5 min and reached a peak by 15-30 min. Insulin also increased the physical association between PKCδ with PKB and with PDK1. The insulin-induced PKCδ-PKB association was PI3K dependent. PKB-PKCδ association was accounted for by the involvement of PDK1. Overexpression of dominant negative PKCδ abrogated insulin-induced association of PKCδ with both PKB and PDK1. Blockade of PKCδ also decreased insulin-induced Thr308 PKB phosphorylation and PKB translocation. Moreover, PKCδ inhibition reduced insulin-induced GSK3 phosphorylation. The results indicate that insulin-activated PKCδ interacts with PDK1 to regulate PKB.

AB - PKCδ has been shown to be activated by insulin and to interact with insulin receptor and IRS. PKB(Akt) plays an important role in glucose transport and glycogen synthesis. In this study, we investigated the possibility that PKCδ may be involved in insulin-induced activation of PKB. Studies were conducted on primary cultures of rat skeletal muscle. PKB was activated by insulin stimulation within 5 min and reached a peak by 15-30 min. Insulin also increased the physical association between PKCδ with PKB and with PDK1. The insulin-induced PKCδ-PKB association was PI3K dependent. PKB-PKCδ association was accounted for by the involvement of PDK1. Overexpression of dominant negative PKCδ abrogated insulin-induced association of PKCδ with both PKB and PDK1. Blockade of PKCδ also decreased insulin-induced Thr308 PKB phosphorylation and PKB translocation. Moreover, PKCδ inhibition reduced insulin-induced GSK3 phosphorylation. The results indicate that insulin-activated PKCδ interacts with PDK1 to regulate PKB.

KW - Glucose uptake

KW - Glycogenesis

KW - Insulin

KW - Insulin signaling

KW - PDK1

KW - Protein kinase B

KW - Protein kinase Cδ

KW - Skeletal muscle

UR - http://www.scopus.com/inward/record.url?scp=33748597111&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2006.08.100

DO - 10.1016/j.bbrc.2006.08.100

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

C2 - 16962999

AN - SCOPUS:33748597111

SN - 0006-291X

VL - 349

SP - 954

EP - 962

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Protein kinase Cδ participates in insulin-induced activation of PKB via PDK1

Abstract

Bibliographical note

Funding

Keywords

Access to Document

Other files and links

Fingerprint

Cite this