ArticleBiophysical journal1995
Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis.
Article in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 57 citations in OpenAlex.
- Article
- The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions.PLoS genetics · 2016Article
- Mechanisms and Functions of Vinculin Interactions with Phospholipids at Cell Adhesion Sites.The Journal of biological chemistry · 2016Review
- Efficient Exploration of Membrane-Associated Phenomena at Atomic Resolution.The Journal of membrane biology · 2015Review
- Membrane-induced structural rearrangement and identification of a novel membrane anchor in talin F2F3.Biophysical journal · 2014Article
- Prediction of lipid-binding sites based on support vector machine and position specific scoring matrix.The protein journal · 2010Article
- CapZ-lipid membrane interactions: a computer analysis.Theoretical biology & medical modelling · 2006Article
- Protein-lipid interactions: correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data.Theoretical biology & medical modelling · 2006Article
- Alpha-catenin: at the junction of intercellular adhesion and actin dynamics.Nature reviews. Molecular cell biology · 2004Review
- Microviscoelasticity of the apical cell surface of human umbilical vein endothelial cells (HUVEC) within confluent monolayers.Biophysical journal · 2004Article
- Opening-up of liposomal membranes by talin.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Acidic phospholipids inhibit the intramolecular association between the N- and C-terminal regions of vinculin, exposing actin-binding and protein kinase C phosphorylation sites.The Biochemical journal · 1996Article
- Vinculin, talin and focal adhesions.Journal of muscle research and cell motility · 1996Review
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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
In recent in vitro experiments, it has been demonstrated that the 47-kDa fragment of the talin molecule and the 32-kDa fragment of the vinculin molecule interact with acidic phospholipids. By using a computer analysis method, we determined the hydrophobic and amphipathic stretches of these fragments and, by applying a purpose-written matrix method, we ascertained the molecular amphipathic structure of alpha-helices. Calculations for the 47-kDa mouse talin fragment (residues 1-433; NH2-terminal region) suggest specific interactions of residues 21-39, 287-342, and 385-406 with acidic phospholipids and a general lipid-binding domain for mouse talin (primary amino acid sequence 385-401) and for Dictyostelium talin (primary amino acid sequence 348-364). Calculations for the 32-kDa chicken embryo vinculin fragment (residues 858-1066; COOH-terminal region) and from nematode vinculin alignment indicate for chicken embryo vinculin residues 935-978 and 1020-1040 interactions with acidic phospholipids. Experimental confirmation has been given for vinculin (residues 916-970), and future detailed experimental analyses are now needed to support the remaining computational data.
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