US-France Cooperative Research:  Molecular Basis of Calcium Cyclic Nucleotide Signal Transduction
{'Code': '01090000', 'Directorate': {'Abbreviation': 'O/D', 'LongName': 'Office Of The Director'}, 'Division': {'Abbreviation': 'OISE', 'LongName': 'Office Of Internatl Science &Engineering'}}
{'SignBlockName': 'Pierre Perrolle', 'PO_EMAI': None, 'PO_PHON': None}
This award will support collaborative research in biochemistry                  between Dr. Daniel Watterson, Vanderbilt University School of                   Medicine, and Dr. Jacques Haiech, Centre de Recherches de                       Biochimie  Macromoleculaire, Montpellier, France.  The objective of             this research is to study the molecular basis of calcium and cylic              nucleotide signal transduction.                                                                                                                                 Calcium and cyclic AMP are two important second messengers in                   eukaryotic cells.  Variations of their concentrations serve as                  intracellular signals. Appropriate receptors (calcium and cAMP                  binding proteins) are key elements in the detection and management              of these signals.  Among the calcium binding proteins involved in               the calcium signal management of eukaryotic cells, calmodulin                   appears to be a prototypical calcium sensor.  Upon calcium binding,             this protein modifies its conformation and interaction with target              proteins, thus transmitting the information to another element in a             molecular cascade that results in a cellular event (e.g.,                       contraction, exocytosis).  Among the target proteins is a                       calmodulin sensitive adenylate cyclase.  The objectives of the                  proposed research projects are:  1) To study the mechanisms of                  calcium binding to calmodulin by using a site-directed mutagenesis              and protein engineering approach.  The investigators will design                isofunctional mutants with a single tryptophan that will be used as             a reporter group in fluorescence studies;  2) To isolate a cDNA                 coding for the adenylate cyclase from Chlamydomonas.  This cDNA                                                       _____________                             will be used to produce an engineered protein in order to study the             interaction between the adenylate cyclase and calmodulin.  Both the             U.S. and French investigators have significant expertise in the                 proposed research area.  Dr. Watterson's laboratory has developed               methods for the mutagenesis of calmodulin, while Dr. Haiech's                   laboratory has the facilities for growing the expressed proteins in             quantity and for the physical analysis of the resulting                         calmodulins.
{'FirstName': 'Daniel', 'LastName': 'Watterson', 'PI_MID_INIT': 'M', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Daniel M Watterson', 'EmailAddress': None, 'NSF_ID': '000266741', 'StartDate': '02/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Vanderbilt University', 'CityName': 'NASHVILLE', 'ZipCode': '372032416', 'PhoneNumber': '6153222631', 'StreetAddress': '110 21ST AVE S', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Tennessee', 'StateCode': 'TN', 'CONGRESSDISTRICT': '05', 'CONGRESS_DISTRICT_ORG': 'TN05', 'ORG_UEI_NUM': 'GTNBNWXJ12D5', 'ORG_LGL_BUS_NAME': 'VANDERBILT UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '5918', 'Text': 'FRANCE'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8815276.xml'}