Cochaperone
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Cochaperone
Co-chaperones are proteins that assist chaperones in protein folding and other functions. Co-chaperones are the non-client binding molecules that assist in protein folding mediated by Hsp70 and Hsp90. They are particularly essential in stimulation of the ATPase activity of these chaperone proteins. There are a great number of different co-chaperones however based on their domain structure most of them fall into two groups: J-domain proteins and tetratricopeptide repeats (TPR). Co-chaperones assist heat shock proteins in the protein folding process. These co-chaperones can function in a number of ways. Primarily co-chaperones are involved in the ATPase functionality of their associated heat shock proteins. Co-chaperones catalyze the hydrolysis ATP to ADP on their respective chaperones which then allows them undergo a large conformational change that allows them to either bind to their substrates with higher affinity or aid in the release of the substrate following protein folding, a ...
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AHSA1
Activator of 90 kDa heat shock protein ATPase homolog 1 is an enzyme that in humans is encoded by the ''AHSA1'' gene. Interactions AHSA1 has been shown to interact with Heat shock protein 90kDa alpha (cytosolic), member A1 Heat shock protein HSP 90-alpha is a protein that in humans is encoded by the ''HSP90AA1'' gene. Function The gene, HSP90AA1, encodes the human stress-inducible 90-kDa heat shock protein alpha (Hsp90A). Complemented by the constitutively expr .... References External links * Further reading * * * * * * * * {{gene-14-stub Co-chaperones ...
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BAG1
BAG family molecular chaperone regulator 1 is a protein that in humans is encoded by the ''BAG1'' gene. Function The oncogene BCL2 is a membrane protein that blocks a step in a pathway leading to apoptosis or programmed cell death. The protein encoded by this gene binds to BCL2 and is referred to as BCL2-associated athanogene. It enhances the anti-apoptotic effects of BCL2 and represents a link between growth factor receptors and anti-apoptotic mechanisms. At least three protein isoforms are encoded by this mRNA through the use of alternative translation initiation sites, including a non- AUG site. Clinical significance BAG gene has been implicated in age related neurodegenerative diseases as Alzheimer's. It has been demonstrated that BAG1 and BAG 3 regulate the proteasomal and lysosomal protein elimination pathways, respectively. * Interactions BAG1 has been shown to interact with: * Androgen receptor, * C-Raf, * Calcitriol receptor, * Glucocorticoid receptor, ...
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Hsp90
Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs. Heat shock proteins, as a class, are among the most highly expressed cellular proteins across all species. As their name implies, heat shock proteins protect cells when stressed by elevated temperatures. They account for 1–2% of total protein in unstressed cells. However, when cells are heated, the fraction of heat shock proteins increases to 4–6% of cellular proteins. Heat shock protein 90 (Hsp90) is one of the most common of the heat-related proteins. The "90" comes from the fact that it has a mass of roughly 90 kilodaltons. A 90 kDa protein is considered fairly large for a non-fibrous protein. Hsp90 is found in bacteria and all branches of eukarya ...
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ST13
Hsc70-interacting protein also known as suppression of tumorigenicity 13 (ST13) is a protein that in humans is encoded by the ''ST13'' gene. Function The protein encoded by this gene is an adaptor protein that mediates the association of the heat shock proteins HSP70 and HSP90. This protein has been shown to be involved in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones. The expression of this gene is reported to be downregulated in colorectal carcinoma tissue suggesting that is a candidate tumor suppressor gene A tumor suppressor gene (TSG), or anti-oncogene, is a gene that regulates a cell during cell division and replication. If the cell grows uncontrollably, it will result in cancer. When a tumor suppressor gene is mutated, it results in a loss or red .... References Further reading * * * * * * * * * * * * * * * * * * {{protein-stub Co-chaperones ...
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Hsp70
The 70 kilodalton heat shock proteins (Hsp70s or DnaK) are a family of conserved ubiquitously expressed heat shock proteins. Proteins with similar structure exist in virtually all living organisms. Intracellularly localized Hsp70s are an important part of the cell's machinery for protein folding, performing chaperoning functions, and helping to protect cells from the adverse effects of physiological stresses. Additionally, membrane-bound Hsp70s have been identified as a potential target for cancer therapies and their extracellularly localized counterparts have been identified as having both membrane-bound and membrane-free structures. Discovery Members of the Hsp70 family are very strongly upregulated by heat stress and toxic chemicals, particularly heavy metals such as arsenic, cadmium, copper, mercury, etc. Heat shock was originally discovered by Ferruccio Ritossa in the 1960s when a lab worker accidentally boosted the incubation temperature of Drosophila (fruit flies). When ...
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AHSA2
AHSA2 also known as AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast) is a human gene which encodes a protein which acts as co-chaperone of Hsp90 (heat shock protein 90). AHSA2 and the related AHSA1 Activator of 90 kDa heat shock protein ATPase homolog 1 is an enzyme that in humans is encoded by the ''AHSA1'' gene. Interactions AHSA1 has been shown to interact with Heat shock protein 90kDa alpha (cytosolic), member A1 Heat shock protein ... belongs to the AHA (Activator of Hsp90 ATPase) family of stress-regulated proteins that bind directly to Hsp90 and are required for Hsp90-dependent activation of client proteins. References {{protein-stub Co-chaperones ...
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SGTA
Small glutamine-rich tetratricopeptide repeat-containing protein alpha is a protein that in humans is encoded by the ''SGTA'' gene. ''SGTA'' orthologs have also been identified in several mammals for which complete genome data are available. Function This gene encodes a protein which is capable of interacting with the major nonstructural protein of parvovirus H-1 and 70-kDa heat shock cognate protein; however, its function is not known. Since this transcript is expressed ubiquitously in various tissues, this protein may serve a housekeeping function. Interactions SGTA has been shown to interact with Growth hormone receptor Growth hormone receptor is a protein that in humans is encoded by the ''GHR'' gene. GHR orthologs have been identified in most mammals. Structure Growth hormone receptor (GHR) is a transmembrane protein consisting of 620 amino acids. The recep .... References Further reading * * * * * * * * * * * * * * * * Co-chaperones ...
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Peptidylprolyl Isomerase D
Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is an enzyme which in humans is encoded by the ''PPID'' gene on chromosome 4. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. In addition, PPID participates in many biological processes, including mitochondrial metabolism, apoptosis, redox, and inflammation, as well as in related diseases and conditions, such as ischemic reperfusion injury, AIDS, and cancer. Structure Like other cyclophilins, PPID forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti-parallel β-strands and capped by two α-helices at the top and bottom. In addition, the β-turns and loops in the strands contribute to the flexibility of the barrel. PPID in particular is composed of 370 residues and shares structural homology with PPIF, FKBP4, a ...
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CDC37
Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the ''CDC37'' gene. The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a HSP90 Co-chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK, as well as eIF-2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases. Interactions CDC37 has been shown to interact with: * CDK4, * HSP90AA1 * IKBKG, * IKK2, and * STK11. Domain architecture CDC37 consists of three structural domains. The N-terminal domain binds to protein kinases. The central domain is the Hsp90 Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabiliz ...
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GrpE
GrpE (''Gro-P'' like protein E) is a bacterial nucleotide exchange factor that is important for regulation of protein folding machinery, as well as the heat shock response. It is a heat-inducible protein and during stress it prevents unfolded proteins from accumulating in the cytoplasm. Accumulation of unfolded proteins in the cytoplasm can lead to cell death. Discovery GrpE is a nucleotide exchange factor that was first discovered by researchers in 1977 as a protein necessary to propagate bacteriophage λ, a virus that infects bacteria by highjacking the bacteria's own replication machinery, in ''Escherichia coli''. By using a genetic screen, researchers knocked out certain genes in E''. coli'' and then tested whether the bacteria was able to replicate, GrpE was found to be crucial to propagation. Since that time, GrpE has been identified in all bacteria and in Archaea where DnaK and DnaJ are present. The crystal structure of GrpE was determined in 1997 at 2.8 Angstrom and id ...
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Snl1
The first season of ''Saturday Night Live'' (then known as ''NBC's Saturday Night'' to avoid confusion with the similarly named variety show hosted by Howard Cosell), an American sketch comedy series, originally aired in the United States on NBC from October 11, 1975, to July 31, 1976. The show served as a vehicle that launched to stardom the careers of a number of major comedians and actors, including Chevy Chase, John Belushi, and Dan Aykroyd. History In 1974, NBC ''Tonight Show'' host Johnny Carson asked that the weekend broadcasts of "Best of Carson" (officially known as ''The Weekend Tonight Show Starring Johnny Carson'') come to an end (''The Tonight Show'' was a 90-minute program at the time), so he could take two weeknights off; NBC would thus air those repeats on those nights rather than feed them to affiliates for broadcast on either Saturdays or Sundays. Given Johnny Carson's undisputed status as the king of late-night television, NBC heard his request as an ultimatu ...
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Sacsin
Sacsin also known as DnaJ homolog subfamily C member 29 (DNAJC29) is a protein that in humans is encoded by the ''SACS'' gene. Sacsin is a Hsp70 co-chaperone. Function This gene consists of nine exons including a gigantic exon spanning more than 12.8k bp. It encodes the sacsin protein, which includes a UBQ region at the N-terminus, a HEPN domain at the C-terminus and a DnaJ region upstream of the HEPN domain. This modular protein is essential for normal mitochondrial network organization. The gene is highly expressed in the central nervous system, also found in skin, skeletal muscles and at low levels in the pancreas. Mutations in this gene result in autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS), a neurodegenerative disorder characterized by early-onset cerebellar ataxia with spasticity and peripheral neuropathy. Clinical significance Autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS) is a very rare neurodegenerative A neurodegene ...
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