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FLASH GENE

Symbol

HSPB8

contributors: mct - updated : 17-12-2010

HGNC name	heat shock 22kDa protein 8
HGNC id	30171

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

EXPRESSION

Type	ubiquitous

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Cardiovascular heart       predominantly Endocrine parathyroid       highly Nervous brain       predominantly Homo sapiens   nerve cranial nerve     predominantly Homo sapiens Reproductive male system prostate       Visual eye       highly

tissue

System Tissue Tissue level 1 Tissue level 2 Level Pubmed Species Stage Rna symbol Muscular striatum skeletal   highly Homo sapiens Nervous central     highly Homo sapiens Nervous peripherous     highly Homo sapiens

cell lineage
cell lines	melanoma cell lines
fluid/secretion

at STAGE

physiological period

pregnancy

Text

placenta

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains	two binding domains (N- and C-terminal) that are specific for different binding partners
	conserved alpha crystallin domain at the C-terminus possessing chaperone activity

conjugated

PhosphoP

mono polymer

homomer , heteromer , dimer

HOMOLOGY

interspecies

homolog to murine Hs22

Homologene

FAMILY	HSP20/alpha crystallin family
	HspB family of molecular chaperones

CATEGORY

chaperone/stress , receptor membrane serine/threonine

SUBCELLULAR LOCALIZATION	intracellular
	intracellular,cytoplasm
	intracellular,nucleus

basic FUNCTION	having protein serine/threonine kinase, heat shock protein, transferase activities
	displays chaperone activity, autokinase activity, and trigger or block apoptosis activity
	interacts with biological membranes and many different proteins, among them glycolytic enzymes and different protein kinases
	possesses chaperonelike activity and prevents aggregation of denatured proteins
	HSPB8 activity is intrinsically dependent on BAG3, a protein that may facilitate the disposal of doomed proteins by stimulating macroautophagy
	responsible for recognizing the misfolded proteins whereas BAG3, at least in part through its proline-rich domain, might recruit and activate the macroautophagy machinery in close proximity to the chaperone-loaded substrates (MID: 18094623)
	bind to unfolded or misfolded proteins and protect them from aggregation
	potential role of HSPB8 in ribonucleoprotein processing
	promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis
	its activity might be implicated in the degradation of several types of neurotoxic proteins accumulating in TARDBP-positive aggregates in most of the cases of sporadic ALS, in some familial ALS not linked to SOD1 mutations, as well as in frontotemporal dementia
	having a role in the autophagic removal of misfolded proteins responsible for neurodegenerative diseases
	for full HSPB8 activity, autophagy was required although, unlike HSPB7, HSPB8 did induce autophagy
	small heat-shock protein implicated in autophagy

CELLULAR PROCESS

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component	homo or heterodimers (HSP22-MKBP and HSP22-HSP27 hetero-dimers involve the N and C termini of HSP22 and HSP27)
	form a stable molecular complex with the chaperone cohort protein BAG3

INTERACTION

DNA

RNA

small molecule

protein	HSPB1 and HSPB2
	interacting with CRYAB and HSPB6
	binds to BAG3 through the hydrophobic groove formed by its strands beta4 and beta8, a region previously known to be responsible for the formation and stability of higher-order oligomers of many sHsps (small Hsps)
	DEAD box protein DDX20 (gemin3, DP103) is an interacting partner of HSPB8

cell & other

REGULATION

ASSOCIATED DISORDERS

corresponding disease(s)

CMT2L

Susceptibility

Variant & Polymorphism

Candidate gene
Marker	defects in HSPB8-mediated autophagy are likely to contribute to CMT2L pathology and their detection in peripheral blood mononuclear cells could be a useful, accessible biomarker for the disease
Therapy target

ANIMAL & CELL MODELS