ArticleThe Journal of biological chemistry2012
A molecular mechanism for the requirement of PAT-4 (integrin-linked kinase (ILK)) for the localization of UNC-112 (Kindlin) to integrin adhesion sites.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 34 citations in OpenAlex.
- Structural basis of kindlin-3 in leukocyte adhesion deficiency III.Journal of thrombosis and haemostasis : JTH · 2026Article
- ILK binding to β1 integrin is indirect and mediated by kindlin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Brief research report: Effects of Pinch deficiency on cartilage homeostasis in adult mice.Frontiers in cell and developmental biology · 2023Article
- Genetic analysis suggests a surface of PAT-4 (ILK) that interacts with UNC-112 (kindlin).G3 (Bethesda, Md.) · 2022Article
- ATP allosterically stabilizes integrin-linked kinase for efficient force generation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Fatty acids impact sarcomere integrity through myristoylation and ER homeostasis.Cell reports · 2021Article
- Missense mutation of a conserved residue in UNC-112 (kindlin) eliminates binding to PAT-4 (ILK).microPublication biology · 2021Article
- Genetic analysis of the interaction between the N- and C-terminal halves of UNC-112 (kindlin).microPublication biology · 2020Article
- Differences in self-association between kindlin-2 and kindlin-3 are associated with differential integrin binding.The Journal of biological chemistry · 2020Article
- Integrin activation by talin, kindlin and mechanical forces.Nature cell biology · 2019Review
- Kindlin-2 interacts with a highly conserved surface of ILK to regulate focal adhesion localization and cell spreading.Journal of cell science · 2018Article
- High-resolution imaging of muscle attachment structures in Caenorhabditis elegans.Cytoskeleton (Hoboken, N.J.) · 2017Article
- Lucky kindlin: A cloverleaf at the integrin tail.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural basis of kindlin-mediated integrin recognition and activation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The extreme C-terminal region of kindlin-2 is critical to its regulation of integrin activation.The Journal of biological chemistry · 2017Article
- Kindlin-2 directly binds actin and regulates integrin outside-in signaling.The Journal of cell biology · 2016Article
- Molecular basis of kindlin-2 binding to integrin-linked kinase pseudokinase for regulating cell adhesion.The Journal of biological chemistry · 2014Article
- Differences in binding to the ILK complex determines kindlin isoform adhesion localization and integrin activation.Journal of cell science · 2014Article
- Suppressor mutations suggest a surface on PAT-4 (Integrin-linked Kinase) that interacts with UNC-112 (Kindlin).The Journal of biological chemistry · 2014Article
- Talin and kindlin: the one-two punch in integrin activation.Frontiers of medicine · 2014Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Caenorhabditis elegans muscle cells attach to basement membrane through adhesion plaques. PAT-3 (β-integrin), UNC-112 (kindlin), and PAT-4 (integrin-linked kinase) are associated with these structures. Genetic analysis indicated that PAT-4 is required for UNC-112 to be properly localized. We investigated the molecular basis of this requirement. We show that the cytoplasmic tail of PAT-3 binds to full-length UNC-112 and that the N- and C-terminal halves of UNC-112 bind to each other. We demonstrate competition between the UNC-112 C-terminal half and PAT-4 for binding to the UNC-112 N-terminal half. The D382V mutation results in lack of binding to PAT-4 and lack of localization to adhesion structures. T346A or E349K mutations, which abolish interaction of the N- and C-terminal halves, permit D382V UNC-112 to localize to adhesion structures. The following model is proposed. UNC-112 exists in closed inactive and open active conformations, and upon binding of PAT-4 to the UNC-112 N-terminal half, UNC-112 is converted into the open state, able to bind to PAT-3.
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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.