The role of Shp2 (PTPN11) in cancer

被引：246

作者：

Mohi, M. Golam

Neel, Benjamin G.

机构：

[1] Harvard Univ, Sch Med, Beth Israel Deaconess Med Ctr, Canc Biol Program,Div Hematol Oncol,Dept Med, Boston, MA 02215 USA

[2] SUNY Upstate Med Univ, Dept Pharmacol, Syracuse, NY 13020 USA

来源：

CURRENT OPINION IN GENETICS & DEVELOPMENT | 2007年 / 17卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/j.gde.2006.12.011

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Tyrosyl phosphorylation, which is controlled by proteintyrosine kinases (PTKs) and protein-tyrosine phosphatases (PTPs), regulates numerous cellular processes. Altered expression and/or mutations in PTKs are linked to many forms of cancer, yet until recently little was known about the roles of PTPs in normal cells or in cancer. Earlier work established that a member of the PTP superfamily, PTEN, is an important tumor suppressor gene. We now know that at least one other PTP, the SH2 domain-containing phosphatase Shp2, is a bona fide oncogene that is mutated in several types of leukemia and hyperactivated by other mechanisms in some solid tumors. Understanding how Shp2 and other PTPs contribute to oncogenesis should provide new insights into pathogenesis and might suggest new targets for antineoplastic drugs.

引用

页码：23 / 30

页数：8

共 51 条

[11] Human somatic PTPN11 mutations induce hematopoietic-cell hypersensitivity to granulocyte-macrophage colony-stimulating factor [J].

Chan, RJ ;

Leedy, MB ;

Munugalavadla, V ;

Voorhorst, CS ;

Li, YJ ;

Yu, MG ;

Kapur, R .

BLOOD, 2005, 105 (09) :3737-3742

[12] SHP-2 phosphatase is required for hematopoietic cell transformation by Bcr-Abl [J].

Chen, Jing ;

Yu, Wen-Mei ;

Daino, Hanako ;

Broxmeyer, Hal E. ;

Druker, Brian J. ;

Qu, Cheng-Kui .

BLOOD, 2007, 109 (02) :778-785

[13] Protein tyrosine phosphatases: mechanisms of catalysis and regulation [J].

Denu, JM ;

Dixon, JE .

CURRENT OPINION IN CHEMICAL BIOLOGY, 1998, 2 (05) :633-641

[14] Hyperactivation of protein kinase B and ERK have discrete effects on survival, proliferation, and cytokine expression in Nf1-deficient myeloid cells [J].

Donovan, S ;

See, W ;

Bonifas, J ;

Stokoe, D ;

Shannon, KM .

CANCER CELL, 2002, 2 (06) :507-514

[15] Juvenile myelomonocytic leukemia: Molecular understanding and prospects for therapy [J].

Emanuel, PD ;

Shannon, KM ;

Castleberry, RP .

MOLECULAR MEDICINE TODAY, 1996, 2 (11) :468-475

[16] Receptor specific downregulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2 [J].

Funakoshi-Tago, Megumi ;

Pelletier, Stephane ;

Matsuda, Tadashi ;

Parganas, Evan ;

Ihle, James N. .

EMBO JOURNAL, 2006, 25 (20) :4763-4772

[17] Oncogenic mechanisms of the Helicobacter pylori CagA protein [J].

Hatakeyama, M .

NATURE REVIEWS CANCER, 2004, 4 (09) :688-694

[18] Crystal structure of the tyrosine phosphatase SHP-2 [J].

Hof, P ;

Pluskey, S ;

Dhe-Paganon, S ;

Eck, MJ ;

Shoelson, SE .

CELL, 1998, 92 (04) :441-450

[19] Leukemia-associate constitutivelv active mutants of SHP2 protein tyrosine phosphatase inhibit NF1 transcriptional activation by the interferon consensus sequence binding protein [J].

Huang, Weiqi ;

Saberwal, Gurveen ;

Horvath, Elizabeth ;

Zhu, Chunliu ;

Lindsey, Stephan ;

Eklund, Elizabeth A. .

MOLECULAR AND CELLULAR BIOLOGY, 2006, 26 (17) :6311-6332

[20] Hyperactivation of p21ras and the hematopoietic-specific Rho GTPase Rac2, cooperate to alter the proliferation of neurofibromin-deficient mast cells in vivo and in vitro [J].

Ingram, DA ;

Hiatt, K ;

King, AJ ;

Fisher, L ;

Shivakumar, R ;

Derstine, C ;

Wenning, MJ ;

Diaz, B ;

Travers, JB ;

Hood, A ;

Marshall, M ;

Williams, DA ;

Clapp, DW .

JOURNAL OF EXPERIMENTAL MEDICINE, 2001, 194 (01) :57-69

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