ArticleThe Biochemical journal1988
A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties.
Article in The Biochemical journal, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- The Annexin A2/S100A10 Complex: The Mutualistic Symbiosis of Two Distinct Proteins.Biomolecules · 2021Review
- The ANXA2/S100A10 Complex-Regulation of the Oncogenic Plasminogen Receptor.Biomolecules · 2021Review
- Annexin 2 has a dual role as regulator and effector of v-Src in cell transformation.The Journal of biological chemistry · 2009Article
- In vivo and in vitro phosphorylation of annexin II in T cells: potential regulation by annexin V.The Biochemical journal · 1995Article
- Purification of cardiac annexin V from the beagle dog heart and changes in its localization in the ischemic rat heart.Heart and vessels · 1994Article
- Annexins: calcium-binding proteins of multi-functional importance?Medical microbiology and immunology · 1991Review
- Probing nucleation, cutting and capping of actin filaments.Journal of muscle research and cell motility · 1989Review
- Annexin II tetramer: structure and function.Molecular and cellular biochemistryReview
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interaction of plasma membrane with the cytoskeleton involves a large number of proteins, among them a 36 kDa protein that was found to be involved in the interaction with actin filaments. We have isolated a 36 kDa protein from bovine aorta as a monomer and in a complex with a 10 kDa protein. Partial amino acid sequence determinations show that the 36 kDa and 10 kDa proteins isolated from bovine aorta are analogous to or identical with corresponding proteins purified from bovine intestine already described by Kristensen, Saris, Hunter, Hicks, Noonan, Glenney & Tack [(1986) Biochemistry 25, 4497-4503]. We report here that the association of the 10 kDa protein with the 36 kDa protein confers specific calmodulin-binding and actin-severing properties on the complex that are not possessed by the 36 kDa monomer alone. These findings suggest that the protein complex could be involved in thin-filament-related structures or could modulate some Ca2+-regulated events mediated by calmodulin.
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