Calcium Regulation of Cytokinin-Stimulated Morphogenesis in Plant Cells
{'Code': '08060200', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'DCB', 'LongName': 'Division of Cellular Biosciences'}}
{'SignBlockName': 'Maryanna P. Henkart', 'PO_EMAI': None, 'PO_PHON': None}
Understanding the control of cell division in plants by                         cytokinins (N6-substituted adenines) is becoming increasingly                   important as a model for cellular regulation in plants.                         Previous research on cytokinin-induced asymmetrical division in                 target caulonema cells of the moss Funaria has implicated a                     spatially controlled rise in intracellular calcium ion                          concentration as a second messenger that activates calmodulin.                  A model for cytokinin stimulation of cell division is proposed                  that suggests that the binding of cytokinin to asymmetrically                   localized plasma membrane receptors on target cells increases                   intracellular calcium from both intracellular and extracellular                 stores leading to calcium-dependent protein kinase activation                   and protein phosphorylation/dephosphorylation.  Both the spatial                and temporal changes in intracellular calcium and the protein                   phosphorylation appear to be involved in the profound                           cytoplasmic rearrangements seen after hormone treatment.  It is                 becoming increasingly clear that covalent modification of                       preexisting proteins by phosphorylation is a major mechanism in                 the regulation of cell growth and differentiation.  Calcium and                 protein phosphorylation may play a synergistic role in cytokinin                control of cellular function.  The goals of the current project                 are to:  1. characterize cytokinin binding sites by                             photoaffinity labeling using 8-azido benzyladenine, 2. analyze                  the localization of cytokinin binding using antibodies directed                 against cytokinins, 3. analyze calcium uptake using                             metallochromic indicators, and 4. monitor the cytoskeletal                      rearrangements, ion changes and phosphorylation patterns after                  hormone treatment.                                                                                                                                              This research will increase our understanding of cytokinin                      signalling, the second messenger role of calcium, and the                       amplification of cellular response by protein phosphorylation                   leading to developmental changes in plants.
{'FirstName': 'Mary Jane', 'LastName': 'Saunders', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Mary Jane Saunders', 'EmailAddress': 'm.j.saunders@csuohio.edu', 'NSF_ID': '000094101', 'StartDate': '08/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of South Florida', 'CityName': 'TAMPA', 'ZipCode': '336205800', 'PhoneNumber': '8139742897', 'StreetAddress': '4202 E FOWLER AVE', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Florida', 'StateCode': 'FL', 'CONGRESSDISTRICT': '15', 'CONGRESS_DISTRICT_ORG': 'FL15', 'ORG_UEI_NUM': 'NKAZLXLL7Z91', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF SOUTH FLORIDA', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1117', 'Text': 'CELLULAR PHYSIOLOGY'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8802011.xml'}