Proteomics

Dataset Information

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Human Tankyrases TAP-LC-MSMS - Proteomic Analysis of the Human Tankyrase Protein Interaction Network Reveals Its Role in Pexophagy


ABSTRACT: Tankyrase 1 (TNKS1) and tankyrase 2 (TNKS2) belong to the poly(ADP-ribose) polymerase (PARP) family of proteins, which use NAD+ to modify substrate proteins with ADP-ribose modifications. Tankyrases are implicated involving in multiple cellular functions, including the telomere length control, Wnt/b-catenin pathway regulation, glucose uptake and cell cycle regulation. Emerging evidences reveal the pathological relevance of tankyrase in diseases and propose these two key enzymes as potential drug targets. However, the cellular functions and regulatory machineries of tankyrases are still largely unknown. Through this proteomic analysis, we not only defined the protein-protein interaction map for the tankyrases which revealed 100~150 high confident interacting proteins for tankyrases in various cellular functions, but also uncovered the novel regulating function of tankyrase in peroxisome homeostasis.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

DISEASE(S): Disease Free

SUBMITTER: Xu Li  

LAB HEAD: Junjie Chen

PROVIDER: PXD004647 | Pride | 2017-07-24

REPOSITORIES: Pride

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Publications

Proteomic Analysis of the Human Tankyrase Protein Interaction Network Reveals Its Role in Pexophagy.

Li Xu X   Han Han H   Zhou Mao-Tian MT   Yang Bing B   Ta Albert Paul AP   Li Nan N   Chen Junjie J   Wang Wenqi W  

Cell reports 20170701 3


Tankyrase 1 (TNKS) and tankyrase 2 (TNKS2) belong to the poly(ADP-ribose) polymerase family of proteins, which use nicotinamide adenine dinucleotide to modify substrate proteins with ADP-ribose modifications. Emerging evidence has revealed the pathological relevance of TNKS and TNKS2, and identified these two enzymes as potential drug targets. However, the cellular functions and regulatory mechanisms of TNKS/2 are still largely unknown. Through a proteomic analysis, we defined the protein-protei  ...[more]

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