Search results for HSPB1

Showing 11 results out of 11

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Protein (5 results from a total of 5)

Identifier: R-HSA-450563
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: HSPB1: P04792
Identifier: R-HSA-5687009
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: HSPB1: P04792
Identifier: R-HSA-5218697
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: HSPB1: P04792
Identifier: R-HSA-5617628
Species: Homo sapiens
Compartment: cilium
Primary external reference: UniProt: IFT25: Q9Y547
Identifier: R-HSA-5625342
Species: Homo sapiens
Compartment: ciliary tip
Primary external reference: UniProt: IFT25: Q9Y547

Interactor (1 results from a total of 1)

Identifier: P15991
Primary external reference: UniProt: P15991

Reaction (4 results from a total of 4)

Identifier: R-HSA-5687121
Species: Homo sapiens
Compartment: cytosol
HSBP1, also known as HSP27, is small actin-binding protein with roles in cytoskeletal regulation as well as other processes. HSBP1 is a substrate for MAPKAPK5 both in vitro and in vivo, and phosphorylation of serine residues stimulates forskolin-induced F-actin rearrangements (Sun et al, 2007; Tak et al, 2007; Gerits et al, 2007; New et al, 1998; Seternes et al, 2004; Kostenko et al, 2009a; Kostenko et al, 2009b; Kostenko et al, 2011a; reviewed in Kostenko et al, 2011b; Kostenko et al, 2012). There are divergent reports about the physiological relevance of HSBP1 phosphorylation on actin polymeriztion and cell motility (Lavoie et al, 1995; Lamalice et al, 2007; Katsogiannou et al, 2014; Rousseau et al, 2000; Doshi et al, 2010; Stohr et al, 2012). Actin cytoskeletal rearrangements through the MAPK4 pathway are controlled in part by the IGF2BP1-mediated downregulation of MAPK4 translation which abrogates MAPKAPK5 activity and HSBP1 phosphorylation (Stohr et al, 2012).
Identifier: R-HSA-5218916
Species: Homo sapiens
Compartment: cytosol
Activated MAP kinase-activated protein kinase (MAPK/MAPKAPK) 2 and 3 in turn phosphorylate heat shock protein beta 1 (HSPB1, HSP27). HSP27 is an actin-capping protein. Its phosphorylation has been proposed to release it from actin filaments, thus allowing addition of actin monomers and elongation of filaments. Phosphorylation-induced conformational changes causes disaggregation of oligomeric complexes of HSP27 and subsequent disassociation from actin filaments, which may result in a higher rate of actin polymerization (Lamalice et al. 2007, Rousseau et al. 2000, Lavoie et al. 1995).
Identifier: R-HSA-5082356
Species: Homo sapiens
Compartment: nucleoplasm
Combination of chromatin immunoprecipitation (ChIP) microarray analysis and time course gene expression microarray analysis with and without siRNA-mediated inhibition of HSF1 showed that human HSF1 can induce the expression of different sets of target genes to maintain a wide range of biological processes (e.g., anti-apoptosis, RNA splicing, ubiquitination)(Page TG et al. 2006; Vihervaara A. et al. 2013). However, HSF1 is best known for rapid stress-induced upregulation of certain genes related to protein folding, such as HSPA1A/HSP70, HSPC/HSP90, HSPB1/HSP27, and DNAJB1/HSP40 (Mosser DD et al. 1988; Trinklein ND et al. 2004a,b; Page TG et al. 2006; Vihervaara A. et al. 2013).

In the nucleus acetylation of Histone H3 is linked to the function of the Elongator complex in transcription (Kim JH et al. 2002). Elongator complex protein 3 (ELP3), a catalytic acetyltransferase subunit of the Elongator complex, has been reported to regulate the transcription of HSP70 gene, and the histone acetyltransferase (HAT) domain of ELP3 is essential for this function (Han Q et al. 2007; Li F et al. 2001).

Identifier: R-HSA-4793819
Species: Homo sapiens
Compartment: nucleoplasm
Stress-induced HSF1 trimerization results in the increased affinity of HSF1 for the heat shock elements (HSE) usually located within promoters of HSF1 target genes (Sarge KD et al. 1993; Wang Y and Morgan WD 1994; Herbomel G et al. 2013). HSEs are highly conserved and consist of contiguous inverted repeats of pentameric sequence nGAAn (i.e., nGAAnnTTCnnGAAn) (Abravaya K et al. 1991; Sarge KD et al. 1993; Cunniff NFA & Morgan WD 1993). The promoters of HSF target genes can contain more than one HSE, suggesting that the HSF1-HSE interaction may occur in cooperative manner when the binding of HSF trimer to HSE facilitates binding of the next HSF1 trimer (Wang Y and Morgan WD 1994).

Replication protein A (RPA), which is involved in DNA metabolism, was shown to support transcription factor access to nucleosomal DNA as a scaffold for HSF1 and a histone chaperone, FACT (Fujimoto M et al. 2012).

Mutagenesis analysis revealed that DNA binding domain of human HSF1 is required for HSF1 binding to HSE and for nuclear stress bodies (nSBs) formation (Westerheide SD et al. 2009; Herbomel G et al. 2013).

While HSF1 can bind to promoters of many genes targets with or without inducing their transcription, it is best known for stress-induced regulatory functions on certain chaperone genes, such as HSPA1A/HSP70, HSPC/HSP90, HSPB1/HSP27, and DNAJB1/HSP40 (Mosser DD et al. 1988; Trinklein ND et al. 2004a,b; Page TG et al. 2006). At the same time, however, the constitutive expression of hsp70, hsp60, BiP/GRP78, and hsp27 in cultured embryonic murine cells was unaffected by the disruption of the hsf1 gene (McMillan et al. 1998). This is additionally supported by findings that the production of HSP70 was not induced after transfection of HSF1 into human epidermoid A431 cells despite the fact that HSF1 was found to bind HSE on hsp70 gene. While HSP70 production was not altered in unstressed cells, the treatment with phorbol 12-myristate 13-acetate (PMA) increased the HSP70 level in A431 cells and reached even higher expression level in HSF1-transfected A431 cells (Ding XZ et al. 1997). Thus, HSF1 is required for stress-induced upregulation of hsp genes while may not be involved in their basal expression (as was shown in higher eukaryotes).

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-4793786
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSEMBL:ENSG00000106211
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