The Mechanism of Nuclear Protein Import: Analysis in Vitro
{'Code': '08070600', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Maryanna P. Henkart', 'PO_EMAI': None, 'PO_PHON': None}
The investigator has developed an in vitro system which                    functions in authentic nuclear import.  With this approach, the                 following results have already been established: 1, nuclear                     import is ATP-dependent and requires an intact nuclear envelope;                2, import is inhibited by wheat germ agglutinin binding to                      nuclear pores (implicating nuclear pore glycoproteins as possible               participants in nucleocytoplasmic transport); and 3, nuclear                    import can be separated into two sequential steps, binding to the               nuclear envelope and translocation through the pore.  Binding is                mediated by the nuclear targeting signal on the translocatable                  protein, and is independent of ATP and is not inhibited by wheat                germ agglutinin.  Translocation, however, requires ATP and is                   inhibitable by the lectin.  During the tenure of this grant, the                investigator will identify and chemically isolate the receptor                  which mediates specific binding of translocatable proteins, using               chemical cross-linking techniques.  Antisera will then be                       prepared against the receptor, and used for immunolocalization                  and functional studies.  Also, the potential for receptor                       heterogeneity will be explored, by competition studies using                    synthetic nuclear targetting signal peptides.                                                                                                                   The communication between nucleus and cytoplasm is a critical                   feature of cellular life.  On the one hand, it is imperative that               the nuclear content of the cell remain segregated from the                      general cytoplasm, in order to permit the highly-ordered                        regulation of gene activity that is typical of eukaryotic cells;                on the other hand, information, enzymatic machinery, and                        structural components must be provided to the nucleus from the                  cytoplasm.  The results of this project will greatly increase our               understanding of how this communication occurs and is regulated.                Such understanding is a necessary prerequisite to experimental                  manipulations of cytoplasm-to-nucleus communication for specific                biotechnical applications.
{'FirstName': 'Donald', 'LastName': 'Newmeyer', 'PI_MID_INIT': 'D', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Donald D Newmeyer', 'EmailAddress': None, 'NSF_ID': '000222777', 'StartDate': '07/15/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Sanford Burnham Prebys Medical Discovery Institute', 'CityName': 'LA JOLLA', 'ZipCode': '920371005', 'PhoneNumber': '8586463157', 'StreetAddress': '10901 N TORREY PINES RD', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '50', 'CONGRESS_DISTRICT_ORG': 'CA50', 'ORG_UEI_NUM': 'PHMKYKKJLQS1', 'ORG_LGL_BUS_NAME': 'SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1114', 'Text': 'Cellular Dynamics and Function'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8819103.xml'}