Phosphotyrosine confers client specificity to Hsp90.
In this issue of Molecular Cell, Mollapour et al. (2010) report a new tyrosine phosphorylation site in Hsp90, which is essential for Hsp90's interaction with a subset of its client proteins, notably protein kinases.
Mayer
Matthias P
MP
Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH-Alliance, Heidelberg 69120, Germany. m.mayer@zmbh.uni-heidelberg.de <m.mayer@zmbh.uni-heidelberg.de>
D018797:Cell Cycle Proteins / Q000737:chemistry; D045744:Cell Line, Tumor; D019281:Dimerization; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D009687:Nuclear Proteins / Q000737:chemistry; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000737:chemistry*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011505:Protein-Tyrosine Kinases / Q000737:chemistry; D034622:RNA Interference; D054875:Ubiquitination
D018797:Cell Cycle Proteins; D018841:HSP90 Heat-Shock Proteins; D009687:Nuclear Proteins; D019000:Phosphotyrosine; D011505:Protein-Tyrosine Kinases; C499349:WEE1 protein, human; D046988:Proteasome Endopeptidase Complex