ArticleThe EMBO journal1990
Chromaffin cell scinderin, a novel calcium-dependent actin filament-severing protein.
Article in The EMBO journal, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 117 citations in OpenAlex.
- Article
- Knock Out of miRNA-30a-5p and Reconstitution of the Actin Network Dynamics Partly Restores the Impaired Terminal Erythroid Differentiation during Blood Pharming.Stem cell reviews and reports · 2025Article
- Autophagy regulation and protein kinase activity of PIK3C3 controls sertoli cell polarity through its negative regulation on SCIN (scinderin).Autophagy · 2023Article
- Scinderin Is a Novel Oncogene for Its Correlates with Poor Prognosis, Immune Infiltrates and Matrix Metalloproteinase-2/9 (MMP2/9) in Glioma.Brain sciences · 2022Article
- MEX3A promotes nasopharyngeal carcinoma progression via the miR-3163/SCIN axis by regulating NF-κB signaling pathway.Cell death & disease · 2022Article
- AHR Signaling Dampens Inflammatory Signature in Neonatal Skin γδ T Cells.International journal of molecular sciences · 2020Article
- Aberrant Scinderin Expression Correlates With Liver Metastasis and Poor Prognosis in Colorectal Cancer.Frontiers in pharmacology · 2019Article
- Scinderin-knockdown inhibits proliferation and promotes apoptosis in human breast carcinoma cells.Oncology letters · 2018Article
- Scinderin is a novel transcriptional target of BRMS1 involved in regulation of hepatocellular carcinoma cell apoptosis.American journal of cancer research · 2018Article
- The actin binding protein scinderin acts in PC12 cells to tether dense-core vesicles prior to secretion.Molecular and cellular neurosciences · 2017Article
- Adseverin mediates RANKL-induced osteoclastogenesis by regulating NFATc1.Experimental & molecular medicine · 2015Article
- Calcium-controlled conformational choreography in the N-terminal half of adseverin.Nature communications · 2015Article
- Activity and Ca²⁺ regulate the mobility of TRPV1 channels in the plasma membrane of sensory neurons.eLife · 2015Article
- Myosin VI small insert isoform maintains exocytosis by tethering secretory granules to the cortical actin.The Journal of cell biology · 2013Article
- Article
- The crystal structure of the C-terminus of adseverin reveals the actin-binding interface.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Myosin II activation and actin reorganization regulate the mode of quantal exocytosis in mouse adrenal chromaffin cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- Duplicated gelsolin family genes in zebrafish: a novel scinderin-like gene (scinla) encodes the major corneal crystallin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2007Article
- Identification of target actin content and polymerization status as a mechanism of tumor resistance after cytolytic T lymphocyte pressure.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Ca(2+)-dependent activator protein for secretion is critical for the fusion of dense-core vesicles with the membrane in calf adrenal chromaffin cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Scinderin, a novel Ca2+-activated actin filament-severing protein, has been purified to homogeneity from bovine adrenal medulla using a combination of several chromatographic procedures. The protein has an apparent mol. wt of 79,600 +/- 450 daltons, three isoforms (pIs 6.0, 6.1 and 6.2) and two Ca2+ binding sites (Kd 5.85 x 10(-7) M, Bmax 0.81 mol Ca2+/mol protein and Kd 2.85 x 10(-6) M, Bmax 1.87 mol Ca2+/mol protein). Scinderin interacts with F-actin in the presence of Ca2+ and produces a decrease in the viscosity of actin gels as a result of F-actin filament severing as demonstrated by electron microscopy. Scinderin is a structurally different protein from chromaffin cell gelsolin, another actin filament-severing protein described. Scinderin and gelsolin have different mol. wts, isoelectric points, amino acid composition and yield different peptide maps after limited proteolytic digestion by either Staphylococcus V8 protease or chymotrypsin. Moreover, scinderin antibodies do not cross-react with gelsolin and gelsolin antibodies fail to recognize scinderin. Immunofluorescence with anti-scinderin demonstrated that this protein is mainly localized in the subplasmalemma region of the chromaffin cell. Immunoblotting tests with the same antibodies indicated that scinderin is also expressed in brain and anterior as well as posterior pituitary. Presence of scinderin and gelsolin, two Ca2+-dependent actin filament-severing proteins in the same tissue, suggests the possibility of synergistic functions by the two proteins in the control of cellular actin filament networks. Alternatively, the actin filament-severing activity of the two proteins might be under the control of different transduction and modulating influences.
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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.