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Acetylation site mapping on TULP3

ABSTRACT: Fig. 2B: Semi-quantitative acetylation level on TULP3 in the presence of either empty pcDNA 3.1(+), Myc-p300, FLAG-PCAF or FLAG-GCN5 following immunoprecipitation.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Olivier Julien Basil Hubbard

PROVIDER: MSV000086358 | MassIVE | Thu Oct 22 10:29:00 BST 2020

REPOSITORIES: MassIVE

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Publications

A conserved acetylation switch enables pharmacological control of tubby-like protein stability.

Kerek Evan M EM Yoon Kevin H KH Luo Shu Y SY Chen Jerry J Valencia Robert R Julien Olivier O Waskiewicz Andrew J AJ Hubbard Basil P BP

The Journal of biological chemistry 20201123

Tubby-like proteins (TULPs) are characterized by a conserved C-terminal domain that binds phosphoinositides. Collectively, mammalian TULP1-4 proteins play essential roles in intracellular transport, cell differentiation, signaling, and motility. Yet, little is known about how the function of these proteins is regulated in cells. Here, we present the protein-protein interaction network of TULP3, a protein that is responsible for the trafficking of G-protein-coupled receptors to cilia and whose ab ...[more]

PMID: 33187986

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