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The role of HSP70 and HSP90 in the trafficking of hIK1
Author(s) -
Pittner Amie Lynn,
White Colleen Annette,
Jones Heather Marie
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.998.22
Subject(s) - hsp90 , immunoprecipitation , hsp70 , microbiology and biotechnology , chaperone (clinical) , co chaperone , chemistry , heat shock protein , cell , ion channel , cell membrane , membrane protein , biophysics , biochemistry , membrane , biology , receptor , gene , medicine , pathology
The ability of proteins to traffic properly to the cell surface requires that they be properly folded in the ER. The cell contains chaperone proteins which assist in this process. Chaperones will bind to both properly assembled proteins and mis‐folded proteins to determine whether they can traffic out of the ER to the plasma membrane or be retained and eventually degraded. Chaperones may also regulate ion channel cell surface expression by retaining improperly folded channels intracellularly. Co‐immunoprecipitation of hIK1 with HSP70 and HSP90 antibodies resulted in co‐assembly of the proteins in an immune‐complex. Inhibitors of the chaperones will decrease association of these proteins with hIK1 and alter protein expression. Recent studies have shown that chaperone related interactions with ion channels is dictated via charged amino acid residues. Similar residues near the hIK1 selective pore possibly regulate hIK1 association with HSP70 and HSP90. These experiments demonstrate the role of HSP's in hIK1 trafficking and cell surface expression.