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We began analyzing https://journals.biologists.com/jcs/article/127/17/3862/54596/Liprin-1-ERC1-and-LL5-define-polarized-and-dynamic, but it redirected us to https://journals.biologists.com/jcs/article/127/17/3862/54596/Liprin-1-ERC1-and-LL5-define-polarized-and-dynamic. The analysis below is for the second page.
Title[redir]:
Liprin-α1, ERC1 and LL5 define polarized and dynamic structures that are implicated in cell migration | Journal of Cell Science | The Company of Biologists
Description:
ABSTRACT. Cell migration during development and metastatic invasion requires the coordination of actin and adhesion dynamics to promote protrusive activity at the front of the cell. The knowledge of the molecular mechanisms required to achieve such coordination is fragmentary. Here, we identify a new functional complex that drives cell motility. ERC1a (an isoform of ERC1) and the LL5 proteins LL5α and LL5β (encoded by PHLDB1 and PHLDB2, respectively) are required, together with liprin-α1, for effective migration and tumor cell invasion, and do so by stabilizing the protrusive activity at the cell front. Depletion of either protein negatively affects invasion, migration on extracellular matrix, lamellipodial persistence and the internalization of active integrin β1 receptors needed for adhesion turnover at the front of the cell. Liprin-α1, ERC1a and LL5 also define new highly polarized and dynamic cytoplasmic structures uniquely localized near the protruding cell edge. Our results indicate that the functional complex and the associated structures described here represent an important mechanism to drive tumor cell migration.
Title[redir]:
Liprin-α1, ERC1 and LL5 define polarized and dynamic structures that are implicated in cell migration | Journal of Cell Science | The Company of Biologists
Description:
ABSTRACT. Cell migration during development and metastatic invasion requires the coordination of actin and adhesion dynamics to promote protrusive activity at the front of the cell. The knowledge of the molecular mechanisms required to achieve such coordination is fragmentary. Here, we identify a new functional complex that drives cell motility. ERC1a (an isoform of ERC1) and the LL5 proteins LL5α and LL5β (encoded by PHLDB1 and PHLDB2, respectively) are required, together with liprin-α1, for effective migration and tumor cell invasion, and do so by stabilizing the protrusive activity at the cell front. Depletion of either protein negatively affects invasion, migration on extracellular matrix, lamellipodial persistence and the internalization of active integrin β1 receptors needed for adhesion turnover at the front of the cell. Liprin-α1, ERC1a and LL5 also define new highly polarized and dynamic cytoplasmic structures uniquely localized near the protruding cell edge. Our results indicate that the functional complex and the associated structures described here represent an important mechanism to drive tumor cell migration.
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Keywords {🔍}
cells, cell, liprinα, erca, proteins, fig, google, scholar, control, llβ, migration, integrin, protrusions, sirnas, results, integrins, active, focal, endogenous, silencing, depletion, migrating, adhesions, effects, protein, supplementary, edge, compared, structures, adhesion, lamellipodia, erc, mda, material, accumulation, dynamic, internalization, transfected, scale, turnover, meansem, localization, gfp, area, biol, llα, clusters, endocytic, internalized, invasion,
Topics {✒️}
ez-link cleavable sulfo-nhs-ss-biotin open pdf gfp-tagged mouse wild-type open menu 1 mg/ml dextran–alexa-fluor-568 pdgf-regulated rab4-dependent recycling biotin–integrin-β1 internalization assay alexa-fluor-conjugated secondary antibodies 10 µg/ml ctxb–alexa-fluor-555 20 µg/ml transferrin–alexa-fluor-647 mcherry–zyxin-positive focal adhesions representative mcherry–zyxin-positive cells alpha/beta heterodimeric receptors relevant liprin-α1-interacting partners article information ligand-bound active conformations gfp–ll5βm-positive dots induced liprin-α1-mediated cell migration gfp–liprin-α1-expressing cells clear f-actin-positive edge cell-surface-labeled β1 integrins assess clathrin-mediated endocytosis label-free quantitative proteomics internalized biotin-labeled integrin anti-integrin-β1 antibodies low-affinity beta1 integrins erc1a-positive dynamic vesicle anti-integrin-β1 pab anti-β1-integrin pab zyxin-positive dots appearing endogenous erc2–liprin-α complexes internalized integrin–antibody complexes mcherry–zyxin-positive area gfp-tagged liprin-α1 wild-type gfp–ll5β jcs fast-track option anti-ll5β antibody recognizes liprin-α1-mediated motility fast-tracked decision making 50 mm tris-hcl ph 8 overexpressing gfp–liprin-α1 view largedownload slide mannose-6-phosphate receptor pab mcherry–zyxin-positive areas gfp–ll5βm-positive dots cell-surface-bound antibodies spinning-disc head paxillin-positive focal adhesions rim-binding proteins regulated erc1a-positive cluster showing
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ScholarlyArticle:
context:https://schema.org
id:https://journals.biologists.com/jcs/article/127/17/3862/54596/Liprin-1-ERC1-and-LL5-define-polarized-and-dynamic
name:Liprin-α1, ERC1 and LL5 define polarized and dynamic structures that are implicated in cell migration
datePublished:2014-09-01
isPartOf:
id:https://journals.biologists.com/jcs/issue/127/17
type:PublicationIssue
issueNumber:17
datePublished:2014-09-01
isPartOf:
id:https://journals.biologists.com/jcs
type:Periodical
name:Journal of Cell Science
issn:
1477-9137
url:https://dx.doi.org/10.1242/jcs.155663
keywords:
Integrin
Invasion
Lamellipodia
Migration
inLanguage:en
copyrightHolder:
copyrightYear:2025
publisher:
author:
name:Astro, Veronica
affiliation:1 Cell Adhesion Unit, San Raffaele Scientific Institute , 20132 Milano , Italy
type:Person
name:Chiaretti, Sara
affiliation:1 Cell Adhesion Unit, San Raffaele Scientific Institute , 20132 Milano , Italy
type:Person
name:Magistrati, Elisa
affiliation:1 Cell Adhesion Unit, San Raffaele Scientific Institute , 20132 Milano , Italy
type:Person
name:Fivaz, Marc
affiliation:3 Duke-NUS Graduate Medical School Singapore , 169857 Singapore
type:Person
name:de Curtis, Ivan
affiliation:1 Cell Adhesion Unit, San Raffaele Scientific Institute , 20132 Milano , Italy 2 San Raffaele University , 20132 Milano , Italy
type:Person
description:ABSTRACT. Cell migration during development and metastatic invasion requires the coordination of actin and adhesion dynamics to promote protrusive activity at the front of the cell. The knowledge of the molecular mechanisms required to achieve such coordination is fragmentary. Here, we identify a new functional complex that drives cell motility. ERC1a (an isoform of ERC1) and the LL5 proteins LL5α and LL5β (encoded by PHLDB1 and PHLDB2, respectively) are required, together with liprin-α1, for effective migration and tumor cell invasion, and do so by stabilizing the protrusive activity at the cell front. Depletion of either protein negatively affects invasion, migration on extracellular matrix, lamellipodial persistence and the internalization of active integrin β1 receptors needed for adhesion turnover at the front of the cell. Liprin-α1, ERC1a and LL5 also define new highly polarized and dynamic cytoplasmic structures uniquely localized near the protruding cell edge. Our results indicate that the functional complex and the associated structures described here represent an important mechanism to drive tumor cell migration.
pageStart:3862
pageEnd:3876
siteName:The Company of Biologists
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headline:Liprin-α1, ERC1 and LL5 define polarized and dynamic structures that are implicated in cell migration
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image:alt:Issue Cover
PublicationIssue:
id:https://journals.biologists.com/jcs/issue/127/17
issueNumber:17
datePublished:2014-09-01
isPartOf:
id:https://journals.biologists.com/jcs
type:Periodical
name:Journal of Cell Science
issn:
1477-9137
Periodical:
id:https://journals.biologists.com/jcs
name:Journal of Cell Science
issn:
1477-9137
Person:
name:Astro, Veronica
affiliation:1 Cell Adhesion Unit, San Raffaele Scientific Institute , 20132 Milano , Italy
name:Chiaretti, Sara
affiliation:1 Cell Adhesion Unit, San Raffaele Scientific Institute , 20132 Milano , Italy
name:Magistrati, Elisa
affiliation:1 Cell Adhesion Unit, San Raffaele Scientific Institute , 20132 Milano , Italy
name:Fivaz, Marc
affiliation:3 Duke-NUS Graduate Medical School Singapore , 169857 Singapore
name:de Curtis, Ivan
affiliation:1 Cell Adhesion Unit, San Raffaele Scientific Institute , 20132 Milano , Italy 2 San Raffaele University , 20132 Milano , Italy
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