Stevan R. Hubbard

Professor, Skirball Institute of Biomolecular Medicine. Department of Biochemistry and Molecular Pharmacology.

Ph.D., 1987 Stanford University

LAB WEBSITE:
S. Hubbard Lab
KEYWORDS:
Signal Transduction, Insulin receptor, JAK2, Protein tyrosine kinase, X-ray crystallography

Contact Information

Skirball Institute of Biomolecular Medicine
540 First Avenue 3rd floor, Lab 4
New York, N.Y. 10016
Office Tel: (212) 263-8938
Lab Tel: (212) 263-2306
Fax: (212) 263-8951
E-mail: stevan.hubbard@med.nyu.edu

Admin Contact

Alberta Chan
Tel: (212) 263-8573
Email: alberta.chan@nyumc.org


Structural and Mechanistic Studies of Protein Tyrosine Kinases

My laboratory is interested in the molecular mechanisms by which the insulin receptor and other receptor tyrosine kinases (RTKs) are activated upon ligand binding, and the structural basis for recruitment of downstream signaling proteins to activated receptors. Members of the RTK family include, among others, the insulin and insulin-like growth factor-1 (IGF1) receptors, fibroblast growth factor receptor, platelet-derived growth factor receptor, and epidermal growth factor receptor. RTKs play critical roles in signal transduction pathways that mediate cell proliferation, differentiation, migration and metabolism, both in organismal development and in adult homeostasis. RTKs have also been implicated in the onset or progression of numerous cancers. We are also studying the molecular mechanisms by which JAK2, a member of the Janus kinase family of non-receptor tyrosine kinases, is regulated. Activating mutations in JAK2 are causative for myeloproliferative neoplasms in humans. The main experimental technique we employ for three-dimensional structure determination is x-ray crystallography.

Selected Publications: 
  • The tyrosine kinase domains of the insulin and IGF1 receptors are functional dimers in the activated state. Cabail MZ, Li S, Lemmon E, Bowen ME, Hubbard SR, and Miller WT. Nat Commun 6:6406 doi: 10.1038/ncomms7406 (2015) [PubMed]
  • Molecular basis for pseudokinase-dependent autoinhibition of JAK2 tyrosine kinase. Shan Y, Gnanasambandan K, Ungureanu D, Kim ET, Hammaren H, Yamashita K, Silvennoinen O, Shaw DE, Hubbard SR. Nat Struct Mol Biol AOP June 11, 2014 [PubMed]
  • Structural basis for the interaction of the adaptor protein Grb14 with activated Ras. Qamra R, Hubbard SR. PLoS ONE 2013 Aug13;8(8):e72473 [PubMed]
  • Crystal structures of the JAK2 pseudokinase domain and the pathogenic mutant V617F. Bandaranayake RM, Ungureanu D, Shan Y, Shaw DE, Silvennoinen O, Hubbard SR. Nat Struct Mol Biol 19, 754-759 (2012) [PubMed]
  •  The pseudokinase domain of JAK2 is a dual-specificity protein kinase that negatively regulates cytokine signaling. Ungureanu D, Wu J, Pekkala T, Niranjan Y, Young C, Jensen ON, Xu CF, Neubert TA, Skoda RC, Hubbard SR, Silvennoinen O. Nat Struct Mol Biol 18, 971-976 (2011) [PubMed]

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