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TitleThe mechanism of kinesin inhibition by kinesin-binding protein.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateNov 30, 2020
AuthorsJoseph Atherton / Jessica Ja Hummel / Natacha Olieric / Julia Locke / Alejandro Peña / Steven S Rosenfeld / Michel O Steinmetz / Casper C Hoogenraad / Carolyn A Moores /
PubMed AbstractSubcellular compartmentalisation is necessary for eukaryotic cell function. Spatial and temporal regulation of kinesin activity is essential for building these local environments via control of ...Subcellular compartmentalisation is necessary for eukaryotic cell function. Spatial and temporal regulation of kinesin activity is essential for building these local environments via control of intracellular cargo distribution. Kinesin-binding protein (KBP) interacts with a subset of kinesins via their motor domains, inhibits their microtubule (MT) attachment, and blocks their cellular function. However, its mechanisms of inhibition and selectivity have been unclear. Here we use cryo-electron microscopy to reveal the structure of KBP and of a KBP-kinesin motor domain complex. KBP is a tetratricopeptide repeat-containing, right-handed α-solenoid that sequesters the kinesin motor domain's tubulin-binding surface, structurally distorting the motor domain and sterically blocking its MT attachment. KBP uses its α-solenoid concave face and edge loops to bind the kinesin motor domain, and selected structure-guided mutations disrupt KBP inhibition of kinesin transport in cells. The KBP-interacting motor domain surface contains motifs exclusively conserved in KBP-interacting kinesins, suggesting a basis for kinesin selectivity.
External linksElife / PubMed:33252036 / PubMed Central
MethodsEM (single particle)
Resolution4.5 - 6.9 Å
Structure data

11338

6zpg

EMDB-11338, PDB-6zpg:
Kinesin binding protein (KBP)
Method: EM (single particle) / Resolution: 4.6 Å

11339

6zph

EMDB-11339, PDB-6zph:
Kinesin binding protein complexed with Kif15 motor domain
Method: EM (single particle) / Resolution: 6.9 Å

11340

6zpi

EMDB-11340, PDB-6zpi:
Microtubule complexed with Kif15 motor domain. Symmetrised asymmetric unit
Method: EM (single particle) / Resolution: 4.5 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-MG:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

ChemComp-TA1:
TAXOL / medication, chemotherapy*YM / Paclitaxel

Source
  • homo sapiens (human)
  • sus scrofa (pig)
  • Pig (pig)
KeywordsMOTOR PROTEIN / Kinesin / microtubules / kinesin binding protein / KBP

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