Genetics and Biochemistry of Ca++-Dependent K+ Channels
{'Code': '08060200', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'DCB', 'LongName': 'Division of Cellular Biosciences'}}
{'SignBlockName': 'Vincent P. Gutschick', 'PO_EMAI': None, 'PO_PHON': None}
The protozoan, Paramecium tetraurelia undergoes a                          behavioral response in the form of backward swimming to a variety               of stimuli.  Backward swimming is correlated with action                        potentials that can be recorded across the surface membrane of                  the organism.  The action potential involves four specific ion                  channels, a voltage-dependent calcium channel, a voltage-                       dependent potassium channel, and two calcium dependent channels,                one that is selective for potassium and the other for sodium.                   The overall goal of this research is to understand the molecular                components involved in the regulation of the calcium-dependent                  potassium channel from Paramecium.  Recent studies using the                    behavioral mutant called pantophobiac have shown that the                       calcium-binding protein, calmodulin, is involved in the                         regulation of the calcium-dependent potassium channel.                          To understand more fully the molecular mechanism of the                         regulation of this channel and the role of the channel in the                   behavior of Paramecium a combined genetic and biochemical                       approach will be taken.  Biochemical changes in pantophobiac                    mutants that affect the channel will be characterized more fully,               and calmodulin-binding proteins involved in channel regulation                  will be isolated and characterized.                                                  Ion channels in cells are generally composed of complexes                  of membrane proteins, and function as gated pores for the                       orderly transport of ions across cell membranes.  Their function,               besides being involved in the behavior of Paramecium, is the                    basis for excitation in nerve and muscle and for the responses of               many cell types to environmental stimuli.  The molecular                        mechanisms by which ion channels function are, as yet, poorly                   understood.  Paramecium provides an excellent system for basic                  studies of ion channels because it can be genetically manipulated               and large numbers ofidentical cells can be obtained to provide                  sufficient material for biochemical studies.  The results of this               research will provide important new information about the                       molecular mechanism of regulation of the calcium-dependent                      potassium channel.
{'FirstName': 'Robert', 'LastName': 'Hinrichsen', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Robert Hinrichsen', 'EmailAddress': 'bhinrich@grove.iup.edu', 'NSF_ID': '000294657', 'StartDate': '09/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Fred Hutchinson Cancer Research Center', 'CityName': 'SEATTLE', 'ZipCode': '981094433', 'PhoneNumber': '2066674868', 'StreetAddress': '1100 FAIRVIEW AVE N J6-300', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Washington', 'StateCode': 'WA', 'CONGRESSDISTRICT': '07', 'CONGRESS_DISTRICT_ORG': 'WA07', 'ORG_UEI_NUM': 'HMSNCM57QNR5', 'ORG_LGL_BUS_NAME': 'FRED HUTCHINSON CANCER RESEARCH CENTER', 'ORG_PRNT_UEI_NUM': 'HMSNCM57QNR5'}
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[{'Code': '1117', 'Text': 'CELLULAR PHYSIOLOGY'}, {'Code': '1141', 'Text': 'PHYSIOLOG & STRUCTURAL SYS'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8706681.xml'}