Inactivating point mutations in the GAP-like domain render ARHGAP36 cytosolic.

Nano, Patricia R.; Johnson, Taylor K.; Kudo, Takamasa; Mooney, Nancie A.; Ni, Jun; Demeter, Janos; Jackson, Peter K.; Chen, James K.

doi:10.1371/journal.pone.0251684.s003

pone.0251684.s003.pdf (3.6 MB)

Inactivating point mutations in the GAP-like domain render ARHGAP36 cytosolic.

journal contribution

posted on 2021-05-17, 17:26 authored by Patricia R. Nano, Taylor K. Johnson, Takamasa Kudo, Nancie A. Mooney, Jun Ni, Janos Demeter, Peter K. Jackson, James K. Chen

(PDF)

History

Usage metrics

Read the peer-reviewed publication

Structure-activity mapping of ARHGAP36 reveals regulatory roles for its GAP homology and C-terminal domains

PLOS ONE

Keywords

ARHGAP 36 isoforms Rho GTPase-activating protein novel ARHGAP 36 antagonist C-terminal domain N-terminal autoinhibitory motif activates Gli transcription factors prolyl oligopeptidase-like protein sites modulates ARHGAP 36 recruitment isoform-specific N-terminal sequences sequencing-based mutagenesis screen ARHGAP 36 regulation ARHGAP 36 C-terminal domains ARHGAP 36 ARHGAP 36 structure-activity landscape GAP homology domain

Licence

CC BY 4.0

Inactivating point mutations in the GAP-like domain render ARHGAP36 cytosolic.

History

Usage metrics

Read the peer-reviewed publication

Categories

Keywords

Licence

Exports