ARHGAP23 is a multidomain RhoGAP-family protein that functions as a cytoplasmic suppressor of RhoA activity at cell-cell junctions PMID:38970683. At adherens junctions in keratinocytes, association of plakophilin 4 (PKP4) with ARHGAP23 reduces its binding to RhoA, thereby restraining cytoplasmic RhoA activation and stress fiber formation; this PKP4 scaffolding spatially restricts where ARHGAP23 acts on RhoA PMID:38970683. ARHGAP23 is also a component of the core VE-cadherin interactome in endothelial cells, binding VE-cadherin independently of intracellular-domain tyrosine phosphorylation PMID:42006337. Beyond these junction-associated roles, the enzymatic GAP activity and domain functions of ARHGAP23 have not been experimentally characterized in the available corpus.
| Year | Confidence | Finding | PMIDs | Journal |
|---|---|---|---|---|
| 2004 | Low | ARHGAP23 (KIAA1501) was identified as a RhoGAP-domain-containing protein with a domain structure consisting of PDZ, Pleckstrin homology (PH), and RhoGAP domains, shared with ARHGAP21 and Xenopus rGAP. Two protein isoforms (1491-aa isoform 1 and 1144-aa isoform 2) arise from alternative splicing involving a 23-bp exon 23 that causes a frameshift and C-terminal truncation in isoform 2. | PMID:15254754 | International journal of oncology |
| 2024 | Medium | ARHGAP23 acts as a Rho suppressor at adherens junctions: association of PKP4 (plakophilin 4) with ARHGAP23 reduced ARHGAP23 binding to RhoA, thereby preventing RhoA activation in the cytoplasm and stress fiber formation. This places ARHGAP23 as a cytoplasmic inhibitor of RhoA activity whose function is spatially regulated by PKP4 scaffolding. | PMID:38970683 | Cellular and molecular life sciences : CMLS |
| 2026 | Low | ARHGAP23 was identified as a component of the core VE-cadherin interactome in endothelial cells, binding VE-cadherin even when its intracellular domain is not tyrosine-phosphorylated, as detected by mass spectrometry-based proteomics. | PMID:42006337 | iScience |