Evidence map›Paper›PMID 9548729›Full record

ArticleThe Journal of cell biology1998

Modulation of beta1A integrin functions by tyrosine residues in the beta1 cytoplasmic domain.

T Sakai, Q Zhang, R Fässler, D F Mosher

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.4field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 107 citations in OpenAlex.

  1. α(M)β(2) integrin-mediated adhesion and motility of IL-5-stimulated eosinophils on periostin.American journal of respiratory cell and molecular biology · 2013
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  12. Beta1 integrin cytoplasmic tyrosines promote skin tumorigenesis independent of their phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2011
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  17. Analysis of conserved residues in the betapat-3 cytoplasmic tail reveals important functions of integrin in multiple tissues.Developmental dynamics : an official publication of the American Association of Anatomists · 2010
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

T SakaiDepartments of Medicine and Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Q Zhang
R Fässler
D F Mosher
Lund University · SEUniversity of Wisconsin–Madison · US

Funding

STUDIES OF FIBRONECTIN AND RELATED GLYCOPROTEINSR01HL021644 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MOSHER, DEANE FREMONT · 1985 to 2010
$3.2M
THROMBOSPONDIN &MAMMARY ENDOTHELIAL CELL PROLIFERATIONR01HL054462 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MOSHER, DEANE FREMONT · 1995 to 2007
$3.1M
NHLBI NIH HHS HL21644NHLBI NIH HHS HL54462NHLBI NIH HHS R01 HL021644NHLBI NIH HHS R01 HL054462
6 · The paper itself

Abstract

beta1A integrin subunits with point mutations of the cytoplasmic domain were expressed in fibroblasts derived from beta1-null stem cells. beta1A in which one or both of the tyrosines of the two NPXY motifs (Y783, Y795) were changed to phenylalanines formed active alpha5 beta1 and alpha6 beta1 integrins that mediated cell adhesion and supported assembly of fibronectin. Mutation of the proline in either motif (P781, P793) to an alanine or of a threonine in the inter-motif sequence (T788) to a proline resulted in poorly expressed, inactive beta1A. Y783,795F cells developed numerous fine focal contacts and exhibited motility on a surface. When compared with cells expressing wild-type beta1A or beta1A with the D759A activating mutation of a conserved membrane-proximal aspartate, Y783, 795F cells had impaired ability to transverse filters in chemotaxis assays. Analysis of cells expressing beta1A with single Tyr to Phe substitutions indicated that both Y783 and Y795 are important for directed migration. Actin-containing microfilaments of Y783,795F cells were shorter and more peripheral than microfilaments of cells expressing wild-type beta1A. These results indicate that change of the phenol side chains in the NPXY motifs to phenyl groups (which cannot be phosphorylated) has major effects on the organization of focal contacts and cytoskeleton and on directed cell motility.

Indexed as

ActinsAmino AcidsAmino Acid SequenceAnimalsAntigens, CDCell AdhesionCell LineCell MovementChemotactic FactorsCytoplasmCytoskeletal ProteinsExtracellular Matrix ProteinsFibroblastsFibronectinsIntegrin alpha5Integrin alpha6ActinsAmino AcidsAntigens, CDChemotactic FactorsCytoskeletal ProteinsExtracellular Matrix ProteinsFibronectinsIntegrin alpha5Integrin alpha6Integrin beta1Tyrosine

Identifiers

PMID9548729
PMCPMC2148458
OpenAlexW1901040110

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.