ArticleMolecular and cellular biochemistry1994
Molecular cloning and functional expression of chromaffin cell scinderin indicates that it belongs to the family of Ca(2+)-dependent F-actin severing proteins.
Article in Molecular and cellular biochemistry, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 44 citations in OpenAlex.
- Comprehensive Analysis Based on the TCGA Database Identified SCIN as a Key DNA Methylation-Driver Gene in Epstein-Barr Virus-Associated Gastric Cancer.Biochemical genetics · 2025Article
- Adseverin knockdown inhibits osteoclastogenesis in RAW264.7 cells.International journal of molecular medicine · 2014Article
- The cortical acto-Myosin network: from diffusion barrier to functional gateway in the transport of neurosecretory vesicles to the plasma membrane.Frontiers in endocrinology · 2013Review
- There is more than one way to model an elephant. Experiment-driven modeling of the actin cytoskeleton.Biophysical journal · 2013Review
- The role of actin remodeling in the trafficking of intracellular vesicles, transporters, and channels: focusing on aquaporin-2.Pflugers Archiv : European journal of physiology · 2008Review
- 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
- In vivo, villin is required for Ca(2+)-dependent F-actin disruption in intestinal brush borders.The Journal of cell biology · 1999Article
- The regulation of neurotransmitter secretion by protein kinase C.Molecular neurobiology · 1998Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Scinderin is a Ca(2+)-dependent actin filament severing protein present in chromaffin cells, platelets and a variety of secretory cells. It has been suggested that scinderin is involved in chromaffin cell F-actin dynamics and that this actin network controls the delivery of secretory vesicles to plasma membrane exocytotic sites. Moreover, scinderin redistribution and activity may be regulated by pH and Ca2+ in resting and stimulated cells. Here we describe the molecular cloning, the nucleotide sequence and the expression of bovine chromaffin cell scinderin cDNA. The fusion protein obtained cross-reacts with native scinderin antibodies and binds phosphatidylserine (PS), phosphatidylinositol 4,5-bisphosphate (PIP2) and actin in a Ca(+)-dependent manner. Antibodies raised against the fusion protein produced the same cellular staining patterns for scinderin as anti-native scinderin. Nucleotide and amino acid sequence analysis indicate that scinderin has six domains each containing three internal sequence motifs, two actin and two PIP2 binding sites and has 63 and 53% homology with gelsolin and villin. These data indicate that scinderin is a novel member of the family of Ca(2+)-dependent F-actin severing proteins which includes gelsolin and villin.
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