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Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosen...

Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosen...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4443381

Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains

About this item

Full title

Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2015-05, Vol.112 (20), p.6371-6376

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Significance Cytoplasmic dynein is the primary minus-end–directed microtubule (MT) motor. It is unclear how dynein coordinates ATP hydrolysis and MT attachment within and between its two motor domains, each containing four AAA+ ATPases (AAA: ATPase associated with various cellular activities), AAA1–4. We characterize how mechanical tension and nucl...

Alternative Titles

Full title

Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4443381

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4443381

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1417422112

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