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

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

ARHGAP36 is an atypical Rho GTPase-activating protein (GAP) family member that drives both spinal cord development and tumorigenesis, acting in part through an N-terminal motif that suppresses protein kinase A and activates Gli transcription factors. ARHGAP36 also contains isoform-specific N-termina...

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Bibliographic Details
Main Authors: Patricia R Nano, Taylor K Johnson, Takamasa Kudo, Nancie A Mooney, Jun Ni, Janos Demeter, Peter K Jackson, James K Chen
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2021-01-01
Series:PLoS ONE
Online Access:https://doi.org/10.1371/journal.pone.0251684

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https://doi.org/10.1371/journal.pone.0251684

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