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| IJCEM Copyright © 2008-All rights reserved. Published by e-Century Publishing Corporation, Madison, WI 53711 |
Int J Clin Exp Med 2(1),17-25;2009
Review Article
SHP-2 tyrosine phosphatase in human diseases
Hong Zheng, Shawn Alter, Cheng-Kui Qu
Department of Medicine, Division of Hematology/Oncology, Case Comprehensive Cancer Center, Case Western Reserve University,
Cleveland, OH 44106.
Received January 15, 2009; accepted January 25, 2009; available online January 30, 2009
Abstract: SHP-2, a ubiquitously expressed Src homology 2 (SH2) domain-containing protein tyrosine phosphatase (PTP), plays a
critical role in physiology and disease. SHP-2 has been clearly demonstrated to be an important molecule in various cytoplasmic
signal transduction pathways. In addition, emerging evidence indicates that SHP-2 may function in the nucleus and in the mitochondria.
However, the signaling mechanisms of SHP-2 are not completely understood. Interestingly, genetic mutations in SHP-2 that either
enhance or inactivate its catalytic activity have been identified in human diseases with overlapping phenotypes. In light of this hint given
by nature, new cell and animal models now provide the opportunity to uncover how this molecule functions in multiple cellular
processes, and more importantly, how its known mutations induce human diseases. (IJCEM901002).
Key Words: SHP-2, tyrosine phosphatase, Src homology 2 domain
Full Text PDF
Address all correspondence to:
Cheng-Kui Qu, MD, PhD
Department of Medicine
Division of Hematology/Oncology
Case Comprehensive Cancer Center
Case Western Reserve University
Cleveland, OH 44106
USA
E-mail: cxq6@case.edu
Review Article
SHP-2 tyrosine phosphatase in human diseases
Hong Zheng, Shawn Alter, Cheng-Kui Qu
Department of Medicine, Division of Hematology/Oncology, Case Comprehensive Cancer Center, Case Western Reserve University,
Cleveland, OH 44106.
Received January 15, 2009; accepted January 25, 2009; available online January 30, 2009
Abstract: SHP-2, a ubiquitously expressed Src homology 2 (SH2) domain-containing protein tyrosine phosphatase (PTP), plays a
critical role in physiology and disease. SHP-2 has been clearly demonstrated to be an important molecule in various cytoplasmic
signal transduction pathways. In addition, emerging evidence indicates that SHP-2 may function in the nucleus and in the mitochondria.
However, the signaling mechanisms of SHP-2 are not completely understood. Interestingly, genetic mutations in SHP-2 that either
enhance or inactivate its catalytic activity have been identified in human diseases with overlapping phenotypes. In light of this hint given
by nature, new cell and animal models now provide the opportunity to uncover how this molecule functions in multiple cellular
processes, and more importantly, how its known mutations induce human diseases. (IJCEM901002).
Key Words: SHP-2, tyrosine phosphatase, Src homology 2 domain
Full Text PDF
Address all correspondence to:
Cheng-Kui Qu, MD, PhD
Department of Medicine
Division of Hematology/Oncology
Case Comprehensive Cancer Center
Case Western Reserve University
Cleveland, OH 44106
USA
E-mail: cxq6@case.edu
