Determining the Phosphorylation Status of Hippo Components YAP and TAZ Using Phos-tag

Rui Chen; Steven W Plouffe; Kun-Liang Guan

doi:10.1007/978-1-4939-8910-2_21

Determining the Phosphorylation Status of Hippo Components YAP and TAZ Using Phos-tag

Methods Mol Biol. 2019:1893:281-287. doi: 10.1007/978-1-4939-8910-2_21.

Authors

Rui Chen¹, Steven W Plouffe¹, Kun-Liang Guan²

Affiliations

¹ Department of Pharmacology and Moores Cancer Center, University of California, La Jolla, CA, USA.
² Department of Pharmacology and Moores Cancer Center, University of California, La Jolla, CA, USA. kuguan@ucsd.edu.

PMID: 30565141
DOI: 10.1007/978-1-4939-8910-2_21

Abstract

Protein phosphorylation is one of the most important posttranslational modifications in cell signaling and regulation. Protein phosphorylation can be detected by site-specific phospho-antibodies, but generating these antibodies can be costly, time-consuming, and difficult. Recently, Phos-tag technology has been developed to detect protein phosphorylation. Here, we describe our method for using Phos-tag gels to compare the phosphorylation status of YAP and TAZ, the most important downstream effectors of the Hippo pathway.

Keywords: Hippo pathway; Phos-tag gel; Phosphorylation; TAZ; YAP.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Acyltransferases
Cell Cycle Proteins
Hippo Signaling Pathway
Humans
Nuclear Proteins / metabolism*
Phosphorylation
Protein Processing, Post-Translational
Protein Serine-Threonine Kinases*
Signal Transduction*
Transcription Factors / metabolism*

Substances

Cell Cycle Proteins
Nuclear Proteins
Transcription Factors
YY1AP1 protein, human
Acyltransferases
TAFAZZIN protein, human
Protein Serine-Threonine Kinases