Literature DB >> 11874471

Mydj2 as a potent partner of hsc70 in mammalian cells.

Petros Bozidis1, Ioannis Lazaridis, Gerassimos N Pagoulatos, Charalampos E Angelidis.   

Abstract

Dj2 is a member of the DnaJ family of proteins, which regulate the chaperoning function of the hsp70s. We isolated a monkey cDNA dj2 clone corresponding to the large mRNA species encoded by the gene. This mRNA differs from the small mRNA produced by the same gene in that it contains a long 3' untranslated region. Both messages were found to be equally stable and to produce the same protein, which is susceptible to farnesylation. Studies in mouse tissues and various cell lines revealed that these messages and their products are differentially expressed. Surprisingly, we found that only the nonfarnesylated form of dj2 is capable of translocating to the cell nucleus, especially after heat shock. Finally, based on protein interaction studies, our results indicate that dj2 is a specific partner for hsc70 and not for hsp70.

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Year:  2002        PMID: 11874471     DOI: 10.1046/j.1432-1033.2002.02807.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  2 in total

1.  Hsp70 translocates to the nuclei and nucleoli, binds to XRCC1 and PARP-1, and protects HeLa cells from single-strand DNA breaks.

Authors:  Polychronis Kotoglou; Alexandros Kalaitzakis; Patra Vezyraki; Theodore Tzavaras; Lampros K Michalis; Francoise Dantzer; Jae U Jung; Charalampos Angelidis
Journal:  Cell Stress Chaperones       Date:  2008-12-17       Impact factor: 3.667

2.  Hsp70 regulates the doxorubicin-mediated heart failure in Hsp70-transgenic mice.

Authors:  Katerina Naka K; Patra Vezyraki; Alexandros Kalaitzakis; Stelios Zerikiotis; Lampros Michalis; Charalampos Angelidis
Journal:  Cell Stress Chaperones       Date:  2014-04-20       Impact factor: 3.667

  2 in total

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