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Cited by 107Cell Adhesion Molecules ResearchCellular Mechanics and InteractionsProtein Kinase Regulation and GTPase Signaling

Kindlin-2 directly binds actin and regulates integrin outside-in signaling

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Bledzka, Kamila, Bialkowska, Katarzyna, Sossey-Alaoui, Khalid, Vaynberg, Julia, Pluskota, Elzbieta, Qin, Jun, Plow, Edward F.·2016·Journal of Cell Biology
DOI 10.1083/jcb.201501006PMC PMC4828686
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Abstract

Reduced levels of kindlin-2 (K2) in endothelial cells derived from K2+/− mice or C2C12 myoblastoid cells treated with K2 siRNA showed disorganization of their actin cytoskeleton and decreased spreading. These marked changes led us to examine direct binding between K2 and actin. Purified K2 interacts with F-actin in cosedimentation and surface plasmon resonance analyses and induces actin aggregation. We further find that the F0 domain of K2 binds actin. A mutation, LK47/AA, within a predicted actin binding site (ABS) of F0 diminishes its interaction with actin by approximately fivefold. Wild-type K2 and K2 bearing the LK47/AA mutation were equivalent in their ability to coactivate integrin αIIbβ3 in a CHO cell system when coexpressed with talin. However, K2-LK47/AA exhibited a diminished ability to support cell spreading and actin organization compared with wild-type K2. The presence of an ABS in F0 of K2 that influences outside-in signaling across integrins establishes a new foundation for considering how kindlins might regulate cellular responses.

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Authors
Bledzka, K., Bialkowska, K., Sossey-Alaoui, K., Vaynberg, J., Pluskota, E., Qin, J., & Plow, E. F.
Affiliations
  • Cleveland Clinic (US)
  • Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195
Corresponding author
Qin, Jun
ORCID
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2016-04-04
Volume
213
Issue
1
Pages
97-108
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.201501006
PMC
PMC4828686
OpenAlex
W2316278724
Cited by
107
References
1
Citations by year
2026: 5 · 2025: 8 · 2024: 7 · 2023: 10 · 2022: 13 · 2021: 11 · 2020: 15 · 2019: 14 · 2018: 7 · 2017: 12 · 2016: 5
FWCI
10.22
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (P01HL073311)
  • National Center for Advancing Translational Sciences (UL1TR000439)
Topics
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords
Kindlin-2, actin binding, integrin αIIbβ3, actin cytoskeleton organization, cell spreading, talin, actin aggregation, endothelial cells, myoblasts
MeSH terms
Actins, Amino Acid Sequence, Animals, Binding Sites, Cell Adhesion, Cell Line, Cricetulus, Cytoskeletal Proteins, HeLa Cells, Humans, Membrane Proteins, Molecular Sequence Data, Neoplasm Proteins, Protein Binding, Signal Transduction, CHO Cells, Talin, Protein Structure, Tertiary, Platelet Glycoprotein GPIIb-IIIa Complex, Cell Line, Tumor, Mice, Human Umbilical Vein Endothelial Cells

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