Scholars@Duke
Timothy Arthur James Haystead

Timothy Arthur James Haystead

Professor of Pharmacology and Cancer Biology
Pharmacology & Cancer Biology
timothy.haystead@dm.duke.edu
Duke Box 3813, Durham, NC 27710
C 118 LSRC, Durham, NC 27708

Featured Works

Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle.

Journal article J Biol Chem · April 25, 2008 Featured Publication In vivo protein kinases A and G (PKA and PKG) coordinately phosphorylate a broad range of substrates to mediate their various physiological effects. The functions of many of these substrates have yet to be defined genetically. Herein we show a role for smo ... Full text Link to item Cite

Characterization of a UBC13 kinase in Plasmodium falciparum.

Journal article Proc Natl Acad Sci U S A · May 8, 2007 Featured Publication Protein kinases are generally recognized as attractive drug targets to treat a variety of human diseases. Recent analysis of the Plasmodium falciparum kinome identified several kinases that are entirely unique to Plasmodium species. The specific functions ... Full text Link to item Cite

Dual kinase-mediated regulation of PITK by CaMKII and GSK3.

Journal article Cell Signal · March 2007 Featured Publication Phosphatase Interactor Targeting K protein (PITK) was previously identified as a novel PP1 targeting subunit implicated in modulating the phosphorylation of the transcriptional regulator heterogeneous nuclear ribonucleoprotein K (hnRNP K) [Kwiek NC, Thacke ... Full text Link to item Cite

ROCK1 phosphorylates and activates zipper-interacting protein kinase.

Journal article J Biol Chem · February 16, 2007 Featured Publication Zipper-interacting protein kinase (ZIPK) regulates Ca(2+)-independent phosphorylation of both smooth muscle (to regulate contraction) and non-muscle myosin (to regulate non-apoptotic cell death) through either phosphorylation and inhibition of myosin phosp ... Full text Link to item Cite

Real-time in vivo proteomic identification of novel kinase substrates in smooth muscle.

Journal article Methods Mol Biol · 2007 Featured Publication Relaxation of smooth muscle can occur through agonists (such as nitric oxide) that activate guanylyl cyclase and stimulate the production of cGMP, activating its target, cGMP-dependent protein kinase (PKG). This kinase can raise the Ca2+ threshold for cont ... Full text Link to item Cite

PITK, a PP1 targeting subunit that modulates the phosphorylation of the transcriptional regulator hnRNP K.

Journal article Cell Signal · October 2006 Featured Publication Protein phosphatase-1 (PP1), through interactions with substrate targeting subunits, plays critical roles in the regulation of numerous cellular processes. Herein, we describe a newly identified regulatory subunit (PITK; Phosphatase Interactor Targeting K ... Full text Link to item Cite

Regulation of zipper-interacting protein kinase activity in vitro and in vivo by multisite phosphorylation.

Journal article J Biol Chem · March 11, 2005 Featured Publication Zipper-interacting protein kinase (ZIPK) is a widely expressed serine/threonine kinase implicated in cell death and smooth muscle contractility, but its mechanism of regulation is unknown. We have identified six phosphorylation sites in ZIPK that regulate ... Full text Link to item Cite

Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides.

Journal article J Biol Chem · August 13, 2004 Featured Publication Regulation of smooth muscle myosin phosphatase (SMPP-1M) is thought to be a primary mechanism for explaining Ca(2+) sensitization/desensitization in smooth muscle. Ca(2+) sensitization induced by activation of G protein-coupled receptors acting through Rho ... Full text Link to item Cite

Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines.

Journal article Biochemistry · April 20, 2004 Featured Publication Quinone oxidoreductase 2 (QR2) purified from human red blood cells was recently shown to be a potential target of the quinoline antimalarial compounds [Graves et al., (2002) Mol. Pharmacol. 62, 1364]. QR2 catalyzes the two-electron reduction of menadione v ... Full text Link to item Cite

Smooth muscle myosin phosphatase-associated kinase induces Ca2+ sensitization via myosin phosphatase inhibition.

Journal article J Biol Chem · June 28, 2002 Featured Publication Smooth muscle calcium sensitization reflects an inhibition of myosin light chain phosphatase (SMPP-1m) activity; however, the underlying mechanisms are not well understood. SMPP-1m activity can be modulated through phosphorylation of the myosin targeting s ... Full text Link to item Cite

Molecular biologist's guide to proteomics.

Journal article Microbiol Mol Biol Rev · March 2002 Featured Publication The emergence of proteomics, the large-scale analysis of proteins, has been inspired by the realization that the final product of a gene is inherently more complex and closer to function than the gene itself. Shortfalls in the ability of bioinformatics to ... Full text Link to item Cite