ArticleThe Biochemical journal1999
Characterization of beta2 (CD18) integrin phosphorylation in phorbol ester-activated T lymphocytes.
Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 37 citations in OpenAlex.
- Aggregatibacter actinomycetemcomitans leukotoxin causes activation of lymphocyte function-associated antigen 1.Cellular microbiology · 2019Article
- Phosphorylation of the α-chain in the integrin LFA-1 enables β2-chain phosphorylation and α-actinin binding required for cell adhesion.The Journal of biological chemistry · 2018Article
- Potato crop as a source of emetic Bacillus cereus and cereulide-induced mammalian cell toxicity.Applied and environmental microbiology · 2013Article
- p21-activated kinase 4 phosphorylation of integrin beta5 Ser-759 and Ser-762 regulates cell migration.The Journal of biological chemistry · 2010Article
- Regulation of integrin activity and signalling.Biochimica et biophysica acta · 2009Review
- Regulation of LFA-1-dependent inflammatory cell recruitment by Cbl-b and 14-3-3 proteins.Blood · 2008Article
- Two distinct cytoplasmic regions of the beta2 integrin chain regulate RhoA function during phagocytosis.The Journal of cell biology · 2006Article
- Specific integrin alpha and beta chain phosphorylations regulate LFA-1 activation through affinity-dependent and -independent mechanisms.The Journal of cell biology · 2005Article
- Micromechanical tests of adhesion dynamics between neutrophils and immobilized ICAM-1.Biophysical journal · 2004Article
- Role of the cytoplasmic tyrosines of beta 1A integrins in transformation by v-src.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Article
Corrections and comments
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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
Integrins are transmembrane proteins involved in cell-cell and cell-extracellular-matrix interactions. The affinity and avidity of integrins for their ligands change in response to cytoplasmic signals. This 'inside-out' activation has been reported to occur also with beta2 integrins (CD18). The beta2 integrin subunit has previously been shown to become phosphorylated in T lymphocytes on cytoplasmic serine and the functionally important threonine residues after treatment with phorbol esters or on triggering of T-cell receptors. We have now characterized the phosphorylation of beta2 integrins in T-cells in more detail. When T-cells were activated by phorbol esters the phosphorylation was mainly on Ser756. After inhibition of serine/threonine phosphatases, phosphorylation was also found in two of the threonine residues in the threonine triplet 758-760 of the beta2 cytoplasmic domain. Activation of T-cells by phorbol esters resulted in phosphorylation in only approx. 10% of the integrin molecules. Okadaic acid increased this phosphorylation to approx. 30% of the beta2 molecules, assuming three phosphorylation sites. This indicates that a strong dynamic phosphorylation exists in serine and threonine residues of the beta2 integrins.
Indexed as
Identifiers
10085235PMC1220135W1993997506What 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.