Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70 (Q24338681)

GOA release 2020-03-11

TPR domain binding

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Hsp90 family chaperone HSP82 YPL240C

GOA release 2020-03-11

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Chaperone function of Hsp90-associated proteins

GOA release 2020-03-11

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3

F Ulrich Hartl

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author name string

Jason C Young

series ordinal

1

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Nicholas J Hoogenraad

series ordinal

2

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language of work or name

English

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publication date

10 January 2003

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published in

Cell

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volume

112

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page(s)

41-50

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issue

1

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cites work

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Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.

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Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes

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Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70.

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The mitochondrial import receptor Tom70: identification of a 25 kDa core domain with a specific binding site for preproteins

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Getting newly synthesized proteins into shape.

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A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

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Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex

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Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex

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MSF, a novel cytoplasmic chaperone which functions in precursor targeting to mitochondria.

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Molecular chaperones in the cytosol: from nascent chain to folded protein

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GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1

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Import and assembly of proteins into mitochondria of mammalian cells

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Effect of deletions within the leader peptide of pre-ornithine transcarbamylase on mitochondrial import

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70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria

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Protein import into mitochondria

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Versatility of the mitochondrial protein import machinery

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Functional cooperation of mitochondrial protein import receptors in yeast.

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Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes

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Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane

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Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

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MOM19, an import receptor for mitochondrial precursor proteins

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A mitochondrial import receptor for the ADP/ATP carrier

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Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors

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Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae

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Import of ADP/ATP carrier into mitochondria: two receptors act in parallel

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BAG-1 modulates the chaperone activity of Hsp70/Hsc70.

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The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria

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Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90

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Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.

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Hsp90: a specialized but essential protein-folding tool

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Role of the ABC transporter Mdl1 in peptide export from mitochondria

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A mitochondrial specific stress response in mammalian cells

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