Interactions of HSP22 (HSPB8) with HSP20, αB-crystallin, and HSPB3

被引:75
作者
Fontaine, JM [1 ]
Sun, XK [1 ]
Benndorf, R [1 ]
Welsh, MJ [1 ]
机构
[1] Univ Michigan, Sch Med, Dept Cell & Dev Biol, Ann Arbor, MI 48109 USA
关键词
HSP22; alpha B-crystallin; HSP20; HSPB3; protein interaction; heat-shock proteins; Forster resonance energy transfer; yeast two hybrid method;
D O I
10.1016/j.bbrc.2005.09.148
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Seven of the 10 mammalian small heat shock proteins (sHSP) are expressed in muscle where they constitute 3% or more of total protein. sHSPs interact with one another, and these interactions are believed to be important for their functions. In cell types expressing multiple sHSPs, it is of interest to know which sHSPs interact with one another. We have previously shown that HSP22 interacts with itself as well as with HSP27, MKBP, and cvHSP. Using yeast two-hybrid assays and Forster resonance energy transfer microscopy, we now show that HSP22 also can interact with two additional members of the sHSP family, alpha B-crystallin and HSP20. We also show that HSP22 is found in HPLC fractions of primate cardiac muscle containing high molecular weight complexes that include alpha B-crystallin and HSP20. Our results suggest that a variety of oligomers composed of different proportions of different sHSPs may form in cell types expressing multiple sHSPs. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:1006 / 1011
页数:6
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