Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex. (Q40473008)

20 September 2017

title

Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex. (English)

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20 September 2017

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Len Neckers

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20 September 2017

Edward Mimnaugh

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20 September 2017

Wanping Xu

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20 September 2017

Xitong Yuan

series ordinal

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20 September 2017

Zhexin Xiang

series ordinal

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20 September 2017

Monica Marcu

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20 September 2017

language of work or name

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9 January 2005

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Nature Structural & Molecular Biology

20 September 2017

published in

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20 September 2017

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20 September 2017

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20 September 2017

page(s)

120-126

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Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

20 September 2017

cites work

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Transferring substrates to the 26S proteasome.

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Hsp90, not Grp94, regulates the intracellular trafficking and stability of nascent ErbB2

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CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.

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Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.

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p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2.

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Identifiers

DOI

10.1038/NSMB885

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20 September 2017

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