Stevan R Hubbard

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Stevan Hubbard

Professor, Department of Biochemistry and Molecular Pharmacology
Coord Structural Biology Program

Contact Info

Address
540-562 First Avenue
New York, NY 10016

212/263-8938
Stevan.Hubbard@med.nyu.edu


Research Summary

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. The main experimental technique we employ for three-dimensional structure determination is x-ray crystallography. 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.

Research Interests

Structural and Mechanistic Studies of Protein Tyrosine Kinases

Histidine phosphorylation relieves copper inhibition in the mammalian potassium channel KCa3.1
Srivastava, Shekhar; Panda, Saswati; Li, Zhai; Fuhs, Stephen R; Hunter, Tony; Thiele, Dennis J; Hubbard, Stevan R; Skolnik, Edward Y. Histidine phosphorylation relieves copper inhibition in the mammalian potassium channel KCa3.1. eLife. 2016 Aug 19;5:?-? (2219562)

The MuSK receptor family
Burden, SJ; Hubbard, SR; Zhang, W; Yumoto, N. The MuSK receptor family IN: Receptor Tyrosine Kinases: Family and Subfamilies. . p.359-372 (1928082)

The insulin and IGF1 receptor kinase domains are functional dimers in the activated state
Cabail, M Zulema; Li, Shiqing; Lemmon, Eric; Bowen, Mark E; Hubbard, Stevan R; Miller, W Todd. The insulin and IGF1 receptor kinase domains are functional dimers in the activated state. Nature communications. 2015 Mar 11;6:6406-6406 (1495912)

The tyrosine kinase domains of the insulin and IGF1 receptors are functional dimers in the activated state
Cabail, Maria; Li, Shiqing; Lemmon, Eric; Bowen, Mark; Hubbard, Stevan; Miller, Todd. The tyrosine kinase domains of the insulin and IGF1 receptors are functional dimers in the activated state [Meeting Abstract]. FASEB journal. 2015 APR;29:?-? (1812532)

ATP binding to the pseudokinase domain of JAK2 is critical for pathogenic activation
Hammaren, Henrik M; Ungureanu, Daniela; Grisouard, Jean; Skoda, Radek C; Hubbard, Stevan R; Silvennoinen, Olli. ATP binding to the pseudokinase domain of JAK2 is critical for pathogenic activation. Proceedings of the National Academy of Sciences of the United States of America (PNAS). 2015 Mar 30;112(15):4642-4647 (1531932)