|
|
|
|
|
|
|
|
|||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
First published online 14 September 2004
doi: 10.1242/jcs.01373
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Research Article |
1 Laboratory of Cell Biology, NHLBI, NIH, 50 South Drive MSC 8017, Bethesda, MD 20892-0301, USA
2 Neurogenetics Branch, NINDS, NIH, 10 Center Drive, MSC 1250, Bethesda, MD 20893-1250, USA
Author for correspondence (e-mail: eisenbee{at}nhlbi.nih.gov)
Accepted 21 June 2004
The molecular chaperone Hsp70 interacts with misfolded proteins and also accumulates in the nucleus during heat shock. Using GFP-Hsp70 and fluorescence recovery after photobleaching, we show that Hsp70 accumulates in the nucleus during heat shock not only because its inflow rate increases but also because of a marked decrease in its outflow rate. Dynamic imaging also shows that GFP-Hsp70 has greatly reduced mobility when it interacts with organelles such as nucleoli in heat-shocked cells or the large inclusions formed from fragments of mutant huntingtin protein. In heat-shocked cells, nucleoplasmic Hsp70 has reduced mobility relative to the cytoplasm, whereas the ATPase-deficient mutant of Hsp70, Hsp70(K71E), is almost completely immobilized both in the nucleoplasm and the cytoplasm. Moreover, the Hsp70 mutant shows reduced mobility in the presence of diffusive huntingtin fragments with expanded polyglutamine repeats. This provides strong evidence that Hsp70 interacts not only with organelles but also with diffusive proteins in the nucleoplasm and cytoplasm during heat shock as well as with diffusive huntingtin fragments.
Key words: Hsp70, Mobility, Heat shock, Huntingtin
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati 
Twitter What's this?
This article has been cited by other articles:
|
|
 |
|
  Qingyan Au, P. Kanchanastit, J. R. Barber, Shi Chung Ng, and B. Zhang High-Content Image-Based Screening for Small-Molecule Chaperone Amplifiers in Heat Shock J Biomol Screen, December 1, 2008; 13(10): 953 - 959. [Abstract] [PDF]
|
|
|
|
 |
|
 J. Hageman, M. J. Vos, M. A. W. H. van Waarde, and H. H. Kampinga Comparison of Intra-organellar Chaperone Capacity for Dealing with Stress-induced Protein Unfolding J. Biol. Chem., November 23, 2007; 282(47): 34334 - 34345. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K.-J. Lee, A. Panzera, D. Rogawski, L. E. Greene, and E. Eisenberg Cellular prion protein (PrPC) protects neuronal cells from the effect of huntingtin aggregation J. Cell Sci., August 1, 2007; 120(15): 2663 - 2671. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D.-w. Lee, X. Wu, E. Eisenberg, and L. E. Greene Recruitment dynamics of GAK and auxilin to clathrin-coated pits during endocytosis J. Cell Sci., September 1, 2006; 119(17): 3502 - 3512. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Marin-Vinader, C. Shin, C. Onnekink, J. L. Manley, and N. H. Lubsen Hsp27 Enhances Recovery of Splicing as well as Rephosphorylation of SRp38 after Heat Shock Mol. Biol. Cell, February 1, 2006; 17(2): 886 - 894. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D.-w. Lee, X. Zhao, F. Zhang, E. Eisenberg, and L. E. Greene Depletion of GAK/auxilin 2 inhibits receptor-mediated endocytosis and recruitment of both clathrin and clathrin adaptors J. Cell Sci., September 15, 2005; 118(18): 4311 - 4321. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D.-w. Lee, X. Zhao, S. Scarselletta, P. J. Schweinsberg, E. Eisenberg, B. D. Grant, and L. E. Greene ATP Binding Regulates Oligomerization and Endosome Association of RME-1 Family Proteins J. Biol. Chem., April 29, 2005; 280(17): 17213 - 17220. [Abstract] [Full Text] [PDF]
|
|
