The Role of HSP70 and Its Co-chaperones in Protein Misfolding, Aggregation and Disease - The Networking of Chaperones by Co-chaperones - page 253

Table 12.1 (continued)

Protein Disease Main phenotypic

features

Chaperone system Function/putative

function

References

SIL1/BAP Marinesco-Sj￶gren

syndrome

Cerebellar ataxia Hsp70 co-chaperone Regulation of BiP medi-

ated protein folding in
the ER

Senderek et al. ( 2005 )

Cataracts Anttonen et al. ( 2005 ,

2008 )

Developmental delay Karim et al. ( 2006 )

Myopathy Eriguchi et al. ( 2008 )

Takahata et al. ( 2010 )

Tim14/DNAJC19 Dilated Cardiomyopathy

with Ataxia (DCMA)

Cardiomyopathy Hsp70 co-chaperone Translocation of

preproteins across the
inner membrane of
mitochondria

Davey et al. ( 2006 )

Cerebellar ataxia Ojala et al. ( 2012 )

Growth failure

HSJ1a/DNAJB2 Distal hereditary motor

neuropathy (dHMN)

Motor neuron degen-
eration in anterior horn
spinal cord

Hsp70 co-chaperone Dual regulation of

protein folding mediated
by J-domain dependent
Hsp70 interaction and
ubiquitylation via UIM
motifs

Blumen et al. ( 2012 )

Muscle weakness and
atrophy

MRJ/DNAJB6 Limb-girdle muscular

dystrophy

Proximal dominant
muscle weakness

Hsp70 co-chaperone Neural stem cell

renewal, reduces the
formation and toxicity
of misfolded protein
aggregates

Harms et al. ( 2012 )