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Li X, Han H, Zhou MT, et al. Proteomic Analysis of the Human Tankyrase Protein Interaction Network Reveals Its Role in Pexophagy. Cell Rep. 2017;20(3):737-749doi: 10.1016/j.celrep.2017.06.077.
Li, X., Han, H., Zhou, M. T., Yang, B., Ta, A. P., Li, N., Chen, J., & Wang, W. (2017). Proteomic Analysis of the Human Tankyrase Protein Interaction Network Reveals Its Role in Pexophagy. Cell reports, 20(3), 737-749. https://doi.org/10.1016/j.celrep.2017.06.077
Li, Xu, et al. "Proteomic Analysis of the Human Tankyrase Protein Interaction Network Reveals Its Role in Pexophagy." Cell reports vol. 20,3 (2017): 737-749. doi: https://doi.org/10.1016/j.celrep.2017.06.077
Li X, Han H, Zhou MT, Yang B, Ta AP, Li N, Chen J, Wang W. Proteomic Analysis of the Human Tankyrase Protein Interaction Network Reveals Its Role in Pexophagy. Cell Rep. 2017 Jul 18;20(3):737-749. doi: 10.1016/j.celrep.2017.06.077. PMID: 28723574.
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Cell Rep. 2017 Jul 18;20(3):737-749. doi: 10.1016/j.celrep.2017.06.077.

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

Cell reports

Xu Li, Han Han, Mao-Tian Zhou, Bing Yang, Albert Paul Ta, Nan Li, Junjie Chen, Wenqi Wang

Affiliations

  1. Department of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
  2. Department of Developmental and Cell Biology, University of California, Irvine, Irvine, CA 92697, USA.
  3. Department of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA. Electronic address: [email protected].
  4. Department of Developmental and Cell Biology, University of California, Irvine, Irvine, CA 92697, USA. Electronic address: [email protected].

PMID: 28723574 DOI: 10.1016/j.celrep.2017.06.077

Abstract

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-protein interaction network for human TNKS/2 and revealed more than 100 high-confidence interacting proteins with numerous biological functions in this network. Finally, through functional validation, we uncovered a role for TNKS/2 in peroxisome homeostasis and determined that this function is independent of TNKS enzyme activities. Our proteomic study of the TNKS/2 protein interaction network provides a rich resource for further exploration of tankyrase functions in numerous cellular processes.

Copyright © 2017 The Authors. Published by Elsevier Inc. All rights reserved.

Keywords: peroxisome; pexophagy; proteomics; tankyrase

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