<<< Full experiment listing


PXD008215 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleAurora B kinase disrupts the extended conformation of lattice-bound Kinesin-13 MCAK
DescriptionWe reveal that MCAK has a compact conformation in solution using cross-linking and electron microscopy. When MCAK is bound to the microtubule ends, it adopts an extended conformation with the N terminus and neck region of MCAK interacting with the microtubule. Also Aurora Bphosphorylation does not alter MCAK conformation in solution. Aurora B interferes with the extended conformation of MCAK on microtubules to decrease the affinity of MCAK for microtubules and reduces its depolymerase activity in a graded fashion.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJuan Zou
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListphosphorylated residue
InstrumentLTQ Orbitrap Velos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02017-11-15 01:32:25ID requested
12019-01-07 09:38:49announced
22019-01-07 23:48:41announcedUpdated publication reference for PubMed record(s): 30578316.
Publication List
McHugh T, Zou J, Volkov VA, Bertin A, Talapatra SK, Rappsilber J, Dogterom M, Welburn JPI, The depolymerase activity of MCAK shows a graded response to Aurora B kinase phosphorylation through allosteric regulation. J Cell Sci, 132(4):(2019) [pubmed]
Keyword List
curator keyword: Biological
submitter keyword: MCAK, Aurora B, microtubules, phosphorylation
Contact List
Prof. Juri Rappsilber
contact affiliationWellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, Scotland, UK Chair of Bioanalytics, Institute of Biotechnology, Technische Universitšt Berlin, Berlin, German
contact emailjuri.rappsilber@ed.ac.uk
lab head
Juan Zou
contact affiliationThe University of Edinburgh
contact emailjzou@ed.ac.uk
dataset submitter
Full Dataset Link List
Dataset FTP location
PRIDE project URI
Repository Record List
[ + ]