Words similar to misfolded
Example sentences for: misfolded
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Therefore, the first possibility is that the presence of Hsp70 and ubiquitin reflects a failed attempt by the cell to eliminate misfolded protein aggregates via the proteasome pathway.
However, there are many case reports describing patients with progressive neurodegenerative disorders of unknown etiology, collectively referred to as neuronal intranuclear inclusion disease [ 77 ] . While these may consist mainly of unidentified poly-Gln or poly-Ala disorders, the present study raises the possibility that some forms of this disease may arise through unexpected mechanisms, perhaps involving mutations in Rab24 or other poorly characterized members of the Rab GTPase family that mediate trafficking of misfolded proteins within autophagosomes and lysosomes.
Although the formation of intranuclear inclusions has not been observed in previous studies of Ras-related GTPases, it is a common feature of several neurodegenerative disorders where abnormal proteins containing poly-Gln tracts are synthesized as a result of CAG codon expansions [ 52 ] . Examples include Huntington's disease (huntingtin) [ 53 54 ] , spinocerebellar ataxia (SCA) types 1 and 3 (ataxin-1 and ataxin-3) [ 55 56 ] and dentatorubral-pallidoluysian atrophy (atrophin-1) [ 57 ] . These poly-Gln protein aggregates typically contain ubiquitin [ 58 ] and members of the Hsp70 chaperone family [ 59 ] , consistent with a proposed pathway for cellular clearance of toxic misfolded proteins.
In addition, the data presented here do not rule out the possibility that Siah may target group I mGluRs to the proteasome should they become damaged, misfolded or should other conditions in the cell warrant mGluR proteolysis.
Indeed, a similar explanation has been invoked to explain the presence of Hsp70 and ubiquitin in nuclear aggregates observed in cells expressing abnormal gene products with poly-Gln tracts, such as huntingtin [ 54 ] and ataxin-1 [ 59 ] . Based on reports that overexpression of chaperones [ 59 62 ] or a dominant-negative form of the ubiquitin-conjugating enzyme [ 63 ] can suppress the formation of poly-Gln protein aggregates, Kaytor and Warren [ 58 ] proposed a three-stage model wherein (i) molecular chaperones initially associate with the misfolded protein, (ii) failure to diminish the pool of misfolded protein leads to aggregation and ubiquitination and (iii) inefficient degradation of the aggregate by the proteasome is manifested by the accumulation of inclusion bodies.
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