ArticleScientific reports2016
Liprin-α1 and ERC1 control cell edge dynamics by promoting focal adhesion turnover.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 57 citations in OpenAlex.
- Liprin-α family proteins and their cellular functions.The Journal of biological chemistry · 2026Review
- Regulation of cell dynamics by rapid integrin transport through the biosynthetic pathway.The Journal of cell biology · 2026Article
- CYRI-B loss promotes enlarged mature focal adhesions and restricts microtubule and ERC1 access to the cell leading edge.Journal of cell science · 2025Article
- Differential PaxillinB dynamics at Dictyostelium cell-substrate adhesions.Biology open · 2025Article
- Submembrane liprin-α1 clusters spatially localize insulin granule fusion.The Journal of cell biology · 2025Article
- Altering the biophysical properties of ERC1/ELKS-driven condensates interferes with cell motility.Communications biology · 2025Article
- Potential phosphorylation of Liprin-α1 at threonine 701 regulates integrin-mediated cell motility.PloS one · 2025Article
- Focal adhesions are controlled by microtubules through local contractility regulation.The EMBO journal · 2024Article
- Dual specificity kinase DYRK3 regulates cell migration by influencing the stability of protrusions.iScience · 2024Article
- Liprin-α1 contributes to oncogenic MAPK signaling by counteracting ERK activity.Molecular oncology · 2024Article
- Talin2 and KANK2 functionally interact to regulate microtubule dynamics, paclitaxel sensitivity and cell migration in the MDA-MB-435S melanoma cell line.Cellular & molecular biology letters · 2023Article
- The Structural Dynamics, Complexity of Interactions, and Functions in Cancer of Multi-SAM Containing Proteins.Cancers · 2023Review
- Interfering with the ERC1-LL5β interaction disrupts plasma membrane-Associated platforms and affects tumor cell motility.PloS one · 2023Article
- A functional interaction between liprin-α1 and B56γ regulatory subunit of protein phosphatase 2A supports tumor cell motility.Communications biology · 2022Article
- Article
- A mathematical analysis of focal adhesion lifetimes and their effect on cell motility.Biophysical journal · 2022Article
- Liprins in oncogenic signaling and cancer cell adhesion.Oncogene · 2021Review
- Reconstructing Boolean network ensembles from single-cell data for unraveling dynamics in the aging of human hematopoietic stem cells.Computational and structural biotechnology journal · 2021Article
- Liprin-α-Mediated Assemblies and Their Roles in Synapse Formation.Frontiers in cell and developmental biology · 2021Review
- Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer.Matrix biology : journal of the International Society for Matrix Biology · 2020Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Liprin-α1 and ERC1 are interacting scaffold proteins regulating the motility of normal and tumor cells. They act as part of plasma membrane-associated platforms at the edge of motile cells to promote protrusion by largely unknown mechanisms. Here we identify an amino-terminal region of the liprin-α1 protein (liprin-N) that is sufficient and necessary for the interaction with other liprin-α1 molecules. Similar to liprin-α1 or ERC1 silencing, expression of the liprin-N negatively affects tumor cell motility and extracellular matrix invasion, acting as a dominant negative by interacting with endogenous liprin-α1 and causing the displacement of the endogenous ERC1 protein from the cell edge. Interfering with the localization of ERC1 at the cell edge inhibits the disassembly of focal adhesions, impairing protrusion. Liprin-α1 and ERC1 proteins colocalize with active integrin β1 clusters distinct from those colocalizing with cytoplasmic focal adhesion proteins, and influence the localization of peripheral Rab7-positive endosomes. We propose that liprin-α1 and ERC1 promote protrusion by displacing cytoplasmic adhesion components to favour active integrin internalization into Rab7-positive endosomes.
Identifiers
What OpenQuestion holds
Registered trials
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.