9 results match your criteria heterocomplexes proper

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Plant SAM-Domain Proteins Start to Reveal Their Roles.

Trends Plant Sci 2017 08 28;22(8):718-725. Epub 2017 Jun 28.

LPCV, CEA, CNRS, INRA, Université Grenoble-Alpes, BIG, 38000 Grenoble, France. Electronic address:

Proteins often act in complexes assembled via protein-protein interaction domains. The sterile alpha motif (SAM) domain is one of the most prominent interaction domains in animals and is present in proteins of diverse functions. This domain allows head-to-tail closed oligomerisation or polymer formation resulting in homo- and/or heterocomplexes that have been shown to be important for proper protein localisation and function. Read More

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Molecular evidence of the involvement of heat shock protein 90 in brassinosteroid signaling in Arabidopsis T87 cultured cells.

Plant Cell Rep 2014 Mar 29;33(3):499-510. Epub 2013 Dec 29.

The United Graduate School of Agricultural Sciences, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan.

Key Message: A closer association of HSP90s with brassinosteroid signaling is suggested by the brassinosteroid-triggered formation of an HSP90-containing macromolecular complex and the direct interaction between HSP90.3 and BES1.

Abstract: Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that is reportedly involved in the proper folding, stabilization, intracellular trafficking, maintenance and degradation of numerous proteins, as well as the facilitation of cellular signaling in various organisms including plants. Read More

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The FtsH protease heterocomplex in Arabidopsis: dispensability of type-B protease activity for proper chloroplast development.

Plant Cell 2010 Nov 9;22(11):3710-25. Epub 2010 Nov 9.

Key Laboratory of Ministry of Education for Cell Proliferation and Differentiation, College of Life Sciences, Peking University, Beijing 100871, China.

FtsH is an ATP-dependent metalloprotease present as a hexameric heterocomplex in thylakoid membranes. Encoded in the Arabidopsis thaliana YELLOW VARIEGATED2 (VAR2) locus, FtsH2 is one isoform among major Type A (FtsH1/5) and Type B (FtsH2/8) isomers. Mutants lacking FtsH2 (var2) and FtsH5 (var1) are characterized by a typical leaf-variegated phenotype. Read More

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November 2010

Regulation of the atrial natriuretic peptide receptor by heat shock protein 90 complexes.

J Biol Chem 2001 Apr 4;276(14):11371-5. Epub 2001 Jan 4.

Department of Pharmacology, University of South Alabama, Mobile, Alabama 36688, USA.

Heat shock protein 90 (hsp90) is a chaperone required for the proper folding and trafficking of many proteins involved in signal transduction. We tested whether hsp90 plays a role as a chaperone for GC-A, the membrane guanylate cyclase that acts as a receptor for atrial natriuretic peptide (ANP). When cultured cells expressing recombinant GC-A were treated with geldanamycin, an inhibitor of hsp90 function, the ANP-stimulated production of cyclic GMP was inhibited. Read More

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Protein-protein and DNA-protein interactions affect the activity of lymphoid-specific IFN regulatory factors.

J Immunol 1999 Dec;163(12):6468-78

Department of Food Engineering and Biotechnology, Technion, Haifa, Israel.

IFN regulatory factors (IRFs) constitute a family of transcription factors that are involved in IFN signaling and the development and differentiation of the immune system. Targeted gene disruption studies in mice assigned their primary role to the immune system. Two lymphoid-specific IRF members, IFN consensus sequence binding protein (ICSBP) and IRF-4, bind target DNA with greater efficiency following interaction with two transcription factors, PU. Read More

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December 1999

The role of DnaJ-like proteins in glucocorticoid receptor.hsp90 heterocomplex assembly by the reconstituted hsp90.p60.hsp70 foldosome complex.

J Biol Chem 1998 Mar;273(13):7358-66

Department of Pharmacology, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.

The glucocorticoid receptor (GR) is recovered from hormone-free cells in a heterocomplex with the molecular chaperone hsp90, which is required to produce the proper folding state for steroid binding. GR.hsp90 heterocomplexes are formed by a multiprotein system that appears to exist in all eukaryotic cells. Read More

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The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors.

Authors:
W B Pratt

Proc Soc Exp Biol Med 1998 Apr;217(4):420-34

Department of Pharmacology, The University of Michigan Medical School, Ann Arbor 48109-0632, USA.

A variety of transcription factors and protein kinases involved in signal transduction are recovered from cells in heterocomplexes containing the abundant protein chaperone hsp90. Genetic studies in yeast have demonstrated that binding of steroid receptors, the dioxin receptor, and some protein kinases to hsp90 is critical for their signal transducing function in vivo. These heterocomplexes are formed by a multiprotein chaperone machinery consisting of at least four ubiquitous proteins--hsp90, hsp70, p60 and p23. Read More

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Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants.

Biochemistry 1996 Dec;35(48):15249-55

Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109, USA.

In animal cell lysates, multiprotein complexes containing hsp90, hsp70, p60, p23, and several immunophilins can assemble steroid receptors and oncogenic protein kinases, such as v-Src and v-Raf, into heterocomplexes that contain hsp90 and either immunophilins or, in the case of protein kinases, p50. The complexes with hsp90 are required for the proper functioning of these signal transduction systems. Wheat germ lysate contains a similar protein folding activity that forms functional steroid receptor complexes with hsp90, but not all the components of this system have been identified. Read More

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December 1996

The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor.

J Biol Chem 1995 Sep;270(35):20479-84

Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109, USA.

We have recently shown that hsp56, the FK506-binding immunophilin component of both the heat shock protein (hsp90.hsp70.hsp56) heterocomplex and the untransformed glucocorticoid receptor heterocomplex, is bound directly to hsp90 (Czar, M. Read More

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September 1995
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