Phosphorylation of the phosphatase PTPROt at Tyr 399 is a molecular switch that controls osteoclast activity and bone mass in vivo-Reference-Cited by-同舟云学术

Phosphorylation of the phosphatase PTPROt at Tyr 399 is a molecular switch that controls osteoclast activity and bone mass in vivo

Published:2019-01-08 Issue:563 Volume:12 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Roth Lee¹^ORCID,Wakim Jean¹^ORCID,Wasserman Elad¹^ORCID,Shalev Moran¹^ORCID,Arman Esther¹,Stein Merle²^ORCID,Brumfeld Vlad³,Sagum Cari A.⁴^ORCID,Bedford Mark T.⁴^ORCID,Tuckermann Jan²^ORCID,Elson Ari¹^ORCID

Affiliation:

1. Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.

2. Institute of Comparative Molecular Endocrinology, University of Ulm, Ulm 89081, Germany.

3. Department of Chemical Research Support, Weizmann Institute of Science, Rehovot 76100, Israel.

4. Department of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Smithville, TX 78957, USA.

Abstract

A phosphoswitch in the tyrosine phosphatase PTPROt determines whether it stimulates or inhibits the kinase Src.

Funder

Cancer Prevention and Research Institute of Texas

Israel Science Foundation

Kekst Family Center for Medical Genetics at the Weizmann Institute

Gutwirth Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference67 articles.

1. Osteoclast differentiation and activation

2. Osteoclasts: What Do They Do and How Do They Do It?

3. The osteoclast and its unique cytoskeleton

4. Podosome organization drives osteoclast-mediated bone resorption

5. Osteoporosis and Bone Mass Disorders: From Gene Pathways to Treatments

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