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DSK2 Phosphorylation

ABSTRACT: We used mass spectrometry to identify sites of DSK2 phosphorylation by BIN2.

OTHER RELATED OMICS DATASETS IN: PRJNA360931

INSTRUMENT(S): Q Exactive

ORGANISM(S): Arabidopsis Thaliana (ncbitaxon:3702)

SUBMITTER: Yanhai Yin & Justin Walley

PROVIDER: MSV000079641 | MassIVE | Fri Apr 08 11:39:00 BST 2016

REPOSITORIES: MassIVE

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Publications

Selective Autophagy of BES1 Mediated by DSK2 Balances Plant Growth and Survival.

Nolan Trevor M TM Brennan Benjamin B Yang Mengran M Chen Jiani J Zhang Mingcai M Li Zhaohu Z Wang Xuelu X Bassham Diane C DC Walley Justin J Yin Yanhai Y

Developmental cell 20170401 1

Plants encounter a variety of stresses and must fine-tune their growth and stress-response programs to best suit their environment. BES1 functions as a master regulator in the brassinosteroid (BR) pathway that promotes plant growth. Here, we show that BES1 interacts with the ubiquitin receptor protein DSK2 and is targeted to the autophagy pathway during stress via the interaction of DSK2 with ATG8, a ubiquitin-like protein directing autophagosome formation and cargo recruitment. Additionally, DS ...[more]

PMID: 28399398

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Expression data from P14 TCR cytotoxic T cells overexpressing HDAC7 phosphorylation deficient mutant

Project description:The present study reports an unbiased analysis of the cytotoxic T cell serine-threonine phosphoproteome using high resolution mass spectrometry. Approximately 2,000 phosphorylations were identified in CTLs of which approximately 450 were controlled by TCR signaling. A significantly overrepresented group of molecules identified in the phosphoproteomic screen were transcription activators, co-repressors and chromatin regulators. A focus on the chromatin regulators revealed that CTLs have high expression of the histone deacetylase HDAC7 but continually phosphorylate and export this transcriptional repressor from the nucleus. HDAC7 dephosphorylation results in its nuclear accumulation and suppressed expression of genes encoding key cytokines, cytokine receptors and adhesion molecules that determine CTL function. The screening of the CTL phosphoproteome thus reveals intrinsic pathways of serine-threonine phosphorylation that target chromatin regulators in CTLs and determine the CTL functional program. We used Affymetrix microarray analysis to explore the molecular basis for the role of HDAC7 in CTLs and the impact of GFP-HDAC7 phosphorylation deficient mutant expression on the CTL transcriptional profile. In vitro generated P14 TCR cytotoxic T cells were retrovirally infected with a construct encoding GFP-HDAC7 phosphorylation deficient mutant, sorted in base of GFP expression (GFP positive and GFP negative) and processed for microarray analysis in three biological replicas.

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