GUIDO GUIDOTTI Higgins Professor of Biochemistry Email: guidotti@fas.harvard.edu Phone: (617) 495-2308 Mail: 7 Divinity Ave, Room 387, Cambridge MA, 02138 Members of the Guidotti Lab History of Biochemistry at Harvard List of Publications from PubMed

Research:

Structure and Function of Membrane Proteins

The function and regulation of membrane proteins involved in the transfer of solutes (channels and transporters) and of information (receptors) across the plasma membrane are the subjects of research in this laboratory.

The particular proteins under study are the insulin receptor, the (Na,K) ATPase, an insulin-activated cation channel, channels and transporters for ATP, and an ecto-apyrase.

Selected Publications:

Boyum, R., and Guidotti, G. Glucose dependent, cAMP mediated ATP efflux from Saccharomyces cerevisiae. Microbiology 143, 1901-1908 (1997).

Booth, J. and Guidotti, G. Phosphate transport in yeast vacuoles. J. Biol. Chem. 272, 20408-20413 (1997).

Coppi, M.V., Compton, L.A., and Guidotti, G. Isoform specific effects of charged residues at the borders of the M1-M2 loop of the Na,K-ATPase a subunit. Biochemistry 38, 2494-2505 (1999).

Grinthal, A., and Guidotti, G. Substitution of His59 converts CD39 apyrase into an ADPase in a quaternary structure dependent manner. Biochemistry 39, 9-16 (2000).

McGeoch, J.E., McGeoch, M.W., Mao, R., and Guidotti, G. Opposing actions of cGMP and calcium on the conductance of the F(0) subunit c pore. Biochem. Biophys. Res. Commun. 274, 35-840 (2000).

Zhong, X., Malhotra, R., and Guidotti, G. Regulation of yeast ectoapyrase Ynd1p activity by activator subunit Vma13p of vacuolar H-ATPase. J. Biol. Chem. 275, 35592- 35599 (2000).

Lee, K., Jung, J., Kim, M., and Guidotti, G. Interaction of the alpha subunit of Na, K- ATPase with cofilin. Biochem. J. 353, 377-385 (2001).

Chen, W., and Guidotti, G. Soluble apyrases release ADP during ATP hydrolysis. Biochem. Biophys. Res. Commun. 282, 90-95 (2001).

Zhong, X., Malhotra, R., Woodruff, R., and Guidotti, G. Mammalian Plasma Membrane Ecto-NTPDase1, CD39, Is Not Active Intracellularly: The N-Glycosylation State of CD39 Correlates with Surface Activity and Localization. J. Biol. Chem. 276, 41518- 41525 (2001).

Chen, W. and Guidotti, G. The Metal Coordination of sCD39 during ATP Hydrolysis. BMC Biochemistry 2, 9 (2001).

Grinthal, A., and Guidotti, G. Transmembrane Domains Confer Different Substrate Specificities and ADP Hydrolysis Mechanisms on CD39, CD39L1, and Chimeras. Biochemistry 41, 1947-1956 (2002).

Wu, J.J., and Guidotti, G. Construction and Characterization of a Monomeric Insulin Receptor. J. Biol. Chem. 277,  27809-27817 (2002)

Zhong, X., Malhotra, R., and Guidotti, G. ATP transport into the Golgi and extracellular  release require Mcd4 protein and the vacuolar H+-ATPase.  J. Biol. Chem. 278, 33436-33444 (2003).