ArticleJournal of cell science2015
The dual structural roles of the membrane distal region of the α-integrin cytoplasmic tail during integrin inside-out activation.
Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Mechanosensing dysregulation in the fibroblast: A hallmark of the aging heart.Ageing research reviews · 2020Review
- Kindlin Assists Talin to Promote Integrin Activation.Biophysical journal · 2020Article
- Integrin α11 cytoplasmic tail is required for FAK activation to initiate 3D cell invasion and ERK-mediated cell proliferation.Scientific reports · 2019Article
- α-Integrins dictate distinct modes of type IV collagen recruitment to basement membranes.The Journal of cell biology · 2019Article
- The interaction of talin with the cell membrane is essential for integrin activation and focal adhesion formation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Autonomous conformational regulation of βProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structure of an extended βBlood · 2018Article
- 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
- The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation.Scientific reports · 2018Article
- A pivotal role for a conserved bulky residue at the α1-helix of the αI integrin domain in ligand binding.The Journal of biological chemistry · 2017Article
- Receptor-mediated cell mechanosensing.Molecular biology of the cell · 2017Review
- The importance of N-glycosylation on βScientific reports · 2017Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Studies on the mechanism of integrin inside-out activation have been focused on the role of β-integrin cytoplasmic tails, which are relatively conserved and bear binding sites for the intracellular activators including talin and kindlin. Cytoplasmic tails for α-integrins share a conserved GFFKR motif at the membrane-proximal region and this forms a specific interface with the β-integrin membrane-proximal region to keep the integrin inactive. The α-integrin membrane-distal regions, after the GFFKR motif, are diverse both in length and sequence and their roles in integrin activation have not been well-defined. In this study, we report that the α-integrin cytoplasmic membrane-distal region contributes to maintaining integrin in the resting state and to integrin inside-out activation. Complete deletion of the α-integrin membrane-distal region diminished talin- and kindlin-mediated integrin ligand binding and conformational change. A proper length and suitable amino acids in α-integrin membrane-distal region was found to be important for integrin inside-out activation. Our data establish an essential role for the α-integrin cytoplasmic membrane-distal region in integrin activation and provide new insights into how talin and kindlin induce the high-affinity integrin conformation that is required for fully functional integrins.
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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.