NDLI: Combining chemical genetics and proteomics to identify protein kinase substrates

Content Provider	PubMed Central
Author	Noah, Dephoure Howson, Russell W. Blethrow, Justin D. Shokat, Kevan M. O'shea, Erin K.
Copyright Year	2005
Abstract	Phosphorylation is a ubiquitous protein modification important for regulating nearly every aspect of cellular biology. Protein kinases are highly conserved and constitute one of the largest gene families. Identifying the substrates of a kinase is essential for understanding its cellular role, but doing so remains a difficult task. We have developed a high-throughput method to identify substrates of yeast protein kinases that employs a collection of yeast strains each expressing a single epitope-tagged protein and a chemical genetic strategy that permits kinase reactions to be performed in native, whole-cell extracts. Using this method, we screened 4,250 strains expressing epitope-tagged proteins and identified 24 candidate substrates of the Pho85–Pcl1 cyclin-dependent kinase, including the known substrate Rvs167. The power of this method to identify true kinase substrates is strongly supported by functional overlap and colocalization of candidate substrates and the kinase, as well as by the specificity of Pho85–Pcl1 for some of the substrates compared with another Pho85-cyclin kinase complex. This method is readily adaptable to other yeast kinases.
Related Links	http://dx.doi.org/10.1073/pnas.0509080102
Ending Page	17945
Page Count	6
Starting Page	17940
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	50
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-12-13
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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

Combining chemical genetics and proteomics to identify protein kinase substrates.

An efficient proteomics method to identify the cellular targets of protein kinase inhibitors

Combining affinity proteomics and network context to identify new phosphatase substrates and adapters in growth pathways

An evolutionary proteomics approach identifies substrates of the cAMP-dependent protein kinase

Current technologies to identify protein kinase substrates in high throughput

Chemical genomic profiling to identify intracellular targets of a multiplex kinase inhibitor

Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination

Development of “substrate-trapping” mutants to identify physiological substrates of protein tyrosine phosphatases

Combining proteomics and transcriptome sequencing to identify active plant-cell-wall-degrading enzymes in a leaf beetle

Combining chemical genetics and proteomics to identify protein kinase substrates

Similar Documents

Combining chemical genetics and proteomics to identify protein kinase substrates.

An efficient proteomics method to identify the cellular targets of protein kinase inhibitors

Combining affinity proteomics and network context to identify new phosphatase substrates and adapters in growth pathways

An evolutionary proteomics approach identifies substrates of the cAMP-dependent protein kinase

Current technologies to identify protein kinase substrates in high throughput

Chemical genomic profiling to identify intracellular targets of a multiplex kinase inhibitor

Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination

Development of “substrate-trapping” mutants to identify physiological substrates of protein tyrosine phosphatases

Combining proteomics and transcriptome sequencing to identify active plant-cell-wall-degrading enzymes in a leaf beetle

Combining chemical genetics and proteomics to identify protein kinase substrates