NDLI: Examining post-translational modification-mediated protein–protein interactions using a chemical proteomics approach

Content Provider	PubMed Central
Author	Li, Xiang Foley, Emily A. Kawashima, Shigehiro A. Molloy, Kelly R. Li, Yinyin Chait, Brian T. Kapoor, Tarun M.
Copyright Year	2013
Abstract	Post-translational modifications (PTM) of proteins can control complex and dynamic cellular processes via regulating interactions between key proteins. To understand these regulatory mechanisms, it is critical that we can profile the PTM-dependent protein–protein interactions. However, identifying these interactions can be very difficult using available approaches, as PTMs can be dynamic and often mediate relatively weak protein–protein interactions. We have recently developed CLASPI (cross-linking-assisted and stable isotope labeling in cell culture-based protein identification), a chemical proteomics approach to examine protein–protein interactions mediated by methylation in human cell lysates. Here, we report three extensions of the CLASPI approach. First, we show that CLASPI can be used to analyze methylation-dependent protein–protein interactions in lysates of fission yeast, a genetically tractable model organism. For these studies, we examined trimethylated histone H3 lysine-9 (H3K9Me3)-dependent protein–protein interactions. Second, we demonstrate that CLASPI can be used to examine phosphorylation-dependent protein–protein interactions. In particular, we profile proteins recognizing phosphorylated histone H3 threonine-3 (H3T3-Phos), a mitotic histone “mark” appearing exclusively during cell division. Our approach identified survivin, the only known H3T3-Phos-binding protein, as well as other proteins, such as MCAK and KIF2A, that are likely to be involved in weak but selective interactions with this histone phosphorylation “mark”. Finally, we demonstrate that the CLASPI approach can be used to study the interplay between histone H3T3-Phos and trimethylation on the adjacent residue lysine 4 (H3K4Me3). Together, our findings indicate the CLASPI approach can be broadly applied to profile protein–protein interactions mediated by PTMs.
Related Links	http://dx.doi.org/10.1002/pro.2210
Starting Page	287
File Format	PDF
ISSN	1469896X
e-ISSN	1469896X
Journal	Protein Science : A Publication of the Protein Society
Issue Number	3
Volume Number	22
Language	English
Publisher	Wiley Subscription Services, Inc., A Wiley Company
Publisher Date	2013-03-01
Access Restriction	Open
Rights Holder	Wiley Subscription Services, Inc., A Wiley Company
Subject Keyword	Proteomics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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

Quantitative Chemical Proteomics Approach To Identify Post- translational Modification-Mediated Protein−Protein Interactions

Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions.

Examining post-translational modification-mediated protein-protein interactions using a chemical proteomics approach.

Capturing Post-Translational Modification-Triggered Protein–Protein Interactions Using Dual Noncanonical Amino Acid Mutagenesis

The increasing role of structural proteomics in cyanobacteria.

Modification-specific proteomics: Strategies for characterization of post-translational modifications using enrichment techniques

Quantitative Chemical Proteomics Approach to Identify Posttranslational Modification-mediated Protein-protein Interactions

Exploring protein lipidation by mass spectrometry-based proteomics.

A Chemical Approach for the Detection of Protein Sulfinylation

Examining post-translational modification-mediated protein–protein interactions using a chemical proteomics approach

Similar Documents

Quantitative Chemical Proteomics Approach To Identify Post- translational Modification-Mediated Protein−Protein Interactions

Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions.

Examining post-translational modification-mediated protein-protein interactions using a chemical proteomics approach.

Capturing Post-Translational Modification-Triggered Protein–Protein Interactions Using Dual Noncanonical Amino Acid Mutagenesis

The increasing role of structural proteomics in cyanobacteria.

Modification-specific proteomics: Strategies for characterization of post-translational modifications using enrichment techniques

Quantitative Chemical Proteomics Approach to Identify Posttranslational Modification-mediated Protein-protein Interactions

Exploring protein lipidation by mass spectrometry-based proteomics.

A Chemical Approach for the Detection of Protein Sulfinylation

Examining post-translational modification-mediated protein–protein interactions using a chemical proteomics approach