NDLI: Novel Roles of Specific Isoforms of Protein Kinase C in Activation of the c-fos Serum Response Element

Content Provider	PubMed Central
Author	Soh, Jae-won Lee, Eun Hae Prywes, Ron Weinstein, I. Bernard
Copyright Year	1999
Abstract	Protein kinase C (PKC) is a multigene family of enzymes consisting of at least 11 isoforms. It has been implicated in the induction of c-fos and other immediate response genes by various mitogens. The serum response element (SRE) in the c-fos promoter is necessary and sufficient for induction of transcription of c-fos by serum, growth factors, and the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA). It forms a complex with the ternary complex factor (TCF) and with a dimer of the serum response factor (SRF). TCF is the target of several signal transduction pathways and SRF is the target of the rhoA pathway. In this study we generated dominant-negative and constitutively active mutants of PKC-α, PKC-δ, PKC-ɛ, and PKC-ζ to determine the roles of individual isoforms of PKC in activation of the SRE. Transient-transfection assays with NIH 3T3 cells, using an SRE-driven luciferase reporter plasmid, indicated that PKC-α and PKC-ɛ, but not PKC-δ or PKC-ζ, mediate SRE activation. TPA-induced activation of the SRE was partially inhibited by dominant negative c-Raf, ERK1, or ERK2, and constitutively active mutants of PKC-α and PKC-ɛ activated the transactivation domain of Elk-1. TPA-induced activation of the SRE was also partially inhibited by a dominant-negative MEKK1. Furthermore, TPA treatment of serum-starved NIH 3T3 cells led to phosphorylation of SEK1, and constitutively active mutants of PKC-α and PKC-ɛ activated the transactivation domain of c-Jun, a major substrate of JNK. Constitutively active mutants of PKC-α and PKC-ɛ could also induce a mutant c-fos promoter which lacks the TCF binding site, and they also induce transactivation activity of the SRF. Furthermore, rhoA-mediated SRE activation was blocked by dominant negative mutants of PKC-α or PKC-ɛ. Taken together, these findings indicate that PKC-α and PKC-ɛ can enhance the activities of at least three signaling pathways that converge on the SRE: c-Raf–MEK1–ERK–TCF, MEKK1-SEK1-JNK-TCF, and rhoA-SRF. Thus, specific isoforms of PKC may play a role in integrating networks of signal transduction pathways that control gene expression.
Starting Page	1313
File Format	PDF
ISSN	10985549
e-ISSN	10985549
Journal	Molecular and Cellular Biology
Issue Number	2
Volume Number	19
Language	English
Publisher	American Society for Microbiology
Publisher Date	1999-02-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Activation of the c-fos serum-response element by the activated c-Ha-ras protein in a manner independent of protein kinase C and cAMP-dependent protein kinase.

Maximal serum stimulation of the c-fos serum response element requires both the serum response factor and a novel binding factor, SRE-binding protein.

Expression cloning of a novel zinc finger protein that binds to the c-fos serum response element.

Cytoskeletal Rearrangements and Transcriptional Activation of c-fos Serum Response Element by Rho-kinase

Two pathways for serum regulation of the c-fos serum response element require specific sequence elements and a minimal domain of serum response factor.

YY1 facilitates the association of serum response factor with the c-fos serum response element.

ras-induced c-fos expression and proliferation in living rat fibroblasts involves C-kinase activation and the serum response element pathway.

Activation of the serum response element and 12-O-tetradecanoylphorbol-13-acetate response element by the activated c-raf-1 protein in a manner independent of protein kinase C.

Activation of IκB Kinase β by Protein Kinase C Isoforms

Novel Roles of Specific Isoforms of Protein Kinase C in Activation of the c-fos Serum Response Element

Similar Documents

Activation of the c-fos serum-response element by the activated c-Ha-ras protein in a manner independent of protein kinase C and cAMP-dependent protein kinase.

Maximal serum stimulation of the c-fos serum response element requires both the serum response factor and a novel binding factor, SRE-binding protein.

Expression cloning of a novel zinc finger protein that binds to the c-fos serum response element.

Cytoskeletal Rearrangements and Transcriptional Activation of c-fos Serum Response Element by Rho-kinase

Two pathways for serum regulation of the c-fos serum response element require specific sequence elements and a minimal domain of serum response factor.

YY1 facilitates the association of serum response factor with the c-fos serum response element.

ras-induced c-fos expression and proliferation in living rat fibroblasts involves C-kinase activation and the serum response element pathway.

Activation of the serum response element and 12-O-tetradecanoylphorbol-13-acetate response element by the activated c-raf-1 protein in a manner independent of protein kinase C.

Activation of IκB Kinase β by Protein Kinase C Isoforms

Novel Roles of Specific Isoforms of Protein Kinase C in Activation of the c-fos Serum Response Element