ArticlePloS one2013
Purification and SAXS analysis of the integrin linked kinase, PINCH, parvin (IPP) heterotrimeric complex.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- 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
- Integrin-linked kinase (ILK): the known vs. the unknown and perspectives.Cellular and molecular life sciences : CMLS · 2022Review
- PINCH1 Promotes Fibroblast Migration in Extracellular Matrices and Influences Their Mechanophenotype.Frontiers in cell and developmental biology · 2022Article
- Tripeptides as Integrin-Linked Kinase Modulating Agents Based on a Protein-Protein Interaction with α-Parvin.ACS medicinal chemistry letters · 2021Article
- Differences in self-association between kindlin-2 and kindlin-3 are associated with differential integrin binding.The Journal of biological chemistry · 2020Article
- Kindlin-2 interacts with a highly conserved surface of ILK to regulate focal adhesion localization and cell spreading.Journal of cell science · 2018Article
- Non-catalytic signaling by pseudokinase ILK for regulating cell adhesion.Nature communications · 2018Article
- Structural insight and flexible features of NS5 proteins from all four serotypes of Dengue virus in solution.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Differences in binding to the ILK complex determines kindlin isoform adhesion localization and integrin activation.Journal of cell science · 2014Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The heterotrimeric protein complex containing the integrin linked kinase (ILK), parvin, and PINCH proteins, termed the IPP complex, is an essential component of focal adhesions, where it interacts with many proteins to mediate signaling from integrin adhesion receptors. Here we conduct a biochemical and structural analysis of the minimal IPP complex, comprising full-length human ILK, the LIM1 domain of PINCH1, and the CH2 domain of α-parvin. We provide a detailed purification protocol for IPP and show that the purified IPP complex is stable and monodisperse in solution. Using small-angle X-ray scattering (SAXS), we also conduct the first structural characterization of IPP, which reveals an elongated shape with dimensions 120×60×40 Å. Flexibility analysis using the ensemble optimization method (EOM) is consistent with an IPP complex structure with limited flexibility, raising the possibility that inter-domain interactions exist. However, our studies suggest that the inter-domain linker in ILK is accessible and we detect no inter-domain contacts by gel filtration analysis. This study provides a structural foundation to understand the conformational restraints that govern the IPP complex.
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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.