ArticleThe Journal of biological chemistry2012
Plant actin-binding protein SCAB1 is dimeric actin cross-linker with atypical pleckstrin homology domain.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- PuCBL9-PuCIPK11 Modulates Stomatal Microfilament Reorganisation in a Phosphorylation-Dependent Manner to Enhance Drought Tolerance in Poplar.Plant, cell & environment · 2026Article
- SCAB1 coordinates sequential CaScience China. Life sciences · 2024Article
- Phosphatidic acid inhibits SCAB1-mediated F-actin bundling inPlant signaling & behavior · 2023Article
- Phosphatidylinositol 3-phosphate regulates SCAB1-mediated F-actin reorganization during stomatal closure in Arabidopsis.The Plant cell · 2022Article
- Controlling the Gate: The Functions of the Cytoskeleton in Stomatal Movement.Frontiers in plant science · 2022Review
- Respiratory Syncytial Virus Matrix (M) Protein Interacts with Actin In Vitro and in Cell Culture.Viruses · 2018Article
- Structural implications of CaScientific reports · 2016Article
- The Role of Phosphodiesterase 12 (PDE12) as a Negative Regulator of the Innate Immune Response and the Discovery of Antiviral Inhibitors.The Journal of biological chemistry · 2015Article
- Structural features of LC8-induced self-association of swallow.Biochemistry · 2013Article
- Bundling actin filaments from membranes: some novel players.Frontiers in plant science · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SCAB1 is a novel plant-specific actin-binding protein that binds, bundles, and stabilizes actin filaments and regulates stomatal movement. Here, we dissected the structure and function of SCAB1 by structural and biochemical approaches. We show that SCAB1 is composed of an actin-binding domain, two coiled-coil (CC) domains, and a fused immunoglobulin and pleckstrin homology (Ig-PH) domain. We determined crystal structures for the CC1 and Ig-PH domains at 1.9 and 1.7 Å resolution, respectively. The CC1 domain adopts an antiparallel helical hairpin that further dimerizes into a four-helix bundle. The CC2 domain also mediates dimerization. At least one of the coiled coils is required for actin binding, indicating that SCAB1 is a bivalent actin cross-linker. The key residues required for actin binding were identified. The PH domain lacks a canonical basic phosphoinositide-binding pocket but can bind weakly to inositol phosphates via a basic surface patch, implying the involvement of inositol signaling in SCAB1 regulation. Our results provide novel insights into the functional organization of SCAB1.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.