title: Structure-functions of HspB1 (Hsp27).
abstract: Human HspB1 (also denoted Hsp27) is a well-known member, together with alphaB-crystallin, of the small heat-shock (or stress) proteins (sHsps) (20-40 kDa). In this chapter, I describe procedures for testing the oligomeric and phosphorylation patterns of HspB1 as well as its interaction with specific partner/client polypeptides using tissue culture cells genetically modified to express different levels of this protein. The procedures have been developed in my laboratory and could be used in any well-established cellular laboratory. In addition, the different procedures presented here could be extended to test the nine other human sHsp members as well as sHsps from other species.
authors: Stress, Chaperons, and Cell Death Laboratory, CNRS UMR 5534, Claude Bernard University Lyon 1, Villeurbanne, France. arrigo@univ-lyon1.fr
authors: André-Patrick
authors: AP
authors: Arrigo
mesh_terms: D002460:Cell Line; D003459:Crystallins / Q000737:chemistry / Q000378:metabolism; D055551:HSP27 Heat-Shock Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D018832:Molecular Chaperones; D010766:Phosphorylation; D055503:Protein Multimerization
chemical_list: D003459:Crystallins; D055551:HSP27 Heat-Shock Proteins; C057725:HSPB1 protein, human; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones