The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions
Open accessAbstract
Focal adhesions are sites of cell-extracellular matrix interactions that function in anchoring stress fibers to the plasma membrane and in adhesion-mediated signal transduction. Both focal adhesion structure and signaling ability involve protein tyrosine phosphorylation. LAR is a broadly expressed transmembrane protein tyrosine phosphatase comprised of a cell adhesion-like ectodomain and two intracellular protein tyrosine phosphatase domains. We have identified a novel cytoplasmic 160 kDa phosphoserine protein termed LAR-interacting protein 1 (LIP.1), which binds to the LAR membrane-distal D2 protein tyrosine phosphatase domain and appears to localize LAR to focal adhesions. Both LAR and LIP.1 decorate the ends of focal adhesions most proximal to the cell nucleus and are excluded from the distal ends of focal adhesions, thus localizing to regions of focal adhesions presumably undergoing disassembly. We propose that LAR and LIP.1 may regulate the disassembly of focal adhesions and thus help orchestrate cell-matrix interactions.
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The core active zone proteins are not specific for active zones or even neurons.
“Interestingly, the core active zone proteins are not specific for active zones, or even neurons.”
From The Presynaptic Active Zone (2012) · cites this paper as Serra-Pagès et al., 1995
The Results section, “LAR and LIP.1 co-localize to focal adhesions” (page unavailable), reports these proteins at focal adhesions in cultured MCF7 cells, supporting a non-neuronal localization for those proteins. The paper does not identify them as core active-zone proteins or establish that core active-zone proteins generally occur outside active zones or neurons. (LLM, conf=0.82)
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- Authors
- Serra‐Pagès, C., Kedersha, N. L., Fazikas, L., Medley, Q., Debant, A., & Streuli, M.
- Affiliations
- Dana-Farber Cancer Institute (US)
- Venue
- The EMBO Journal
- Published
- 1995-06-01
- Volume
- 14
- Issue
- 12
- Pages
- 2827-2838
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC398401
- OpenAlex
- W1527739697
- Cited by
- 321
- References
- 0
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 3 · 2023: 8 · 2022: 10 · 2021: 9 · 2020: 7 · 2019: 8 · 2018: 4 · 2017: 9 · 2016: 6 · 2015: 6 · 2014: 9 · 2013: 6 · 2012: 7
- FWCI
- 7.69
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (CA-55547, R01CA055547)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- focal adhesions, protein tyrosine phosphatase, coiled-coil proteins, focal adhesion disassembly, cell-matrix interactions, stress fibers, protein phosphorylation, subcellular localization
- MeSH terms
- Amino Acid Sequence, Cell Adhesion, Cloning, Molecular, Cytoplasm, Extracellular Matrix, Humans, Molecular Sequence Data, Molecular Weight, Organ Specificity, Phosphoproteins, Protein Conformation, Receptors, Cell Surface, Recombinant Fusion Proteins, RNA, Messenger, Protein Tyrosine Phosphatases, Sequence Analysis, DNA, Protein Structure, Secondary, Adaptor Proteins, Signal Transducing, Receptor-Like Protein Tyrosine Phosphatases, Class 4
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