NDLI: The pro-apoptotic kinase Mst1 and its caspase cleavage products are direct inhibitors of Akt1

Content Provider	PubMed Central
Author	Cinar, Bekir Fang, Ping-ke Lutchman, Mohini Dolores, Di Vizio Adam, Rosalyn M. Pavlova, Natalya Rubin, Mark A. Yelick, Pamela C. Freeman, Michael R.
Copyright Year	2007
Abstract	Akt kinases mediate cell growth and survival. Here, we report that a pro-apoptotic kinase, Mst1/STK4, is a physiological Akt1 interaction partner. Mst1 was identified as a component of an Akt1 multiprotein complex isolated from lipid raft-enriched fractions of LNCaP human prostate cancer cells. Endogenous Mst1, along with its paralog, Mst2, acted as inhibitors of endogenous Akt1. Surprisingly, mature Mst1 as well as both of its caspase cleavage products, which localize to distinct subcellular compartments and are not structurally homologous, complexed with and inhibited Akt1. cRNAs encoding full-length Mst1, and N- and C-terminal caspase Mst1 cleavage products, reverted an early lethal phenotype in zebrafish development induced by expression of membrane-targeted Akt1. Mst1 and Akt1 localized to identical subcellular sites in human prostate tumors. Mst1 levels declined with progression from clinically localized to hormone refractory disease, coinciding with an increase in Akt activation with transition from hormone naïve to hormone-resistant metastases. These results position Mst1/2 within a novel branch of the phosphoinositide 3-kinase/Akt pathway and suggest an important role in cancer progression.
Related Links	http://dx.doi.org/10.1038/sj.emboj.7601872
Ending Page	4534
Page Count	12
Starting Page	4523
File Format	PDF
ISSN	02614189
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	21
Volume Number	26
Language	English
Publisher	Nature Publishing Group
Publisher Date	2007-10-31
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine 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

Caspase-mediated activation and induction of apoptosis by the mammalian Ste20-like kinase Mst1.

Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation

p53 facilitates pRb cleavage in IL-3-deprived cells: novel pro-apoptotic activity of p53.

Direct inhibition of caspase 3 is dispensable for the anti-apoptotic activity of XIAP

Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases.

Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells.

IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases.

Direct cleavage of the human DNA fragmentation factor-45 by granzyme B induces caspase-activated DNase release and DNA fragmentation

Induction of a pro-apoptotic ATM–NF-κB pathway and its repression by ATR in response to replication stress

The pro-apoptotic kinase Mst1 and its caspase cleavage products are direct inhibitors of Akt1

Similar Documents

Caspase-mediated activation and induction of apoptosis by the mammalian Ste20-like kinase Mst1.

Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation

p53 facilitates pRb cleavage in IL-3-deprived cells: novel pro-apoptotic activity of p53.

Direct inhibition of caspase 3 is dispensable for the anti-apoptotic activity of XIAP

Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases.

Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells.

IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases.

Direct cleavage of the human DNA fragmentation factor-45 by granzyme B induces caspase-activated DNase release and DNA fragmentation

Induction of a pro-apoptotic ATM–NF-κB pathway and its repression by ATR in response to replication stress

The pro-apoptotic kinase Mst1 and its caspase cleavage products are direct inhibitors of Akt1