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Cited by 70Protein Kinase Regulation and GTPase SignalingCellular Mechanics and InteractionsCellular transport and secretion

Myosin I Links PIP 3 Signaling to Remodeling of the Actin Cytoskeleton in Chemotaxis

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Chen, Chun-Lin, Wang, Yu, Sesaki, Hiromi, Iijima, Miho·2012·Science Signaling
DOI 10.1126/scisignal.2002446PMC PMC3381520
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Abstract

A subset of myosin motor proteins binds the membrane phospholipid PIP 3 to link membrane and cytoskeletal dynamics.

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  • Interactions of proteins with PI(3,4,5)P3 and PI(3,4)P2 not mediated by PH domains or related modules have been described, for example specific isoforms of myosin motor proteins.

    “Interactions of proteins with these lipids, not mediated by the PH-domains or related modules, have also been described; one example are specific isoforms of the myosin motor proteins [82,83].”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [82]

    The Results show that specific myosin I isoforms bind PI(3,4,5)P3 and weakly bind PI(3,4)P2. But they also show that mutations in the PH domain of myosin IE’s TH1 region inhibit PI(3,4,5)P3 binding; the Results likewise identify a PH-like sequence involved in human myosin IF binding. Thus this paper does not support using these myosins as examples of interactions unmediated by PH domains or related modules. (LLM, conf=0.88)

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Research works printed but not linked: 37

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Cited by

Sorted by citations

Authors
Chen, C.-L., Wang, Y., Sesaki, H., & Iijima, M.
Affiliations
Johns Hopkins University (US)
Corresponding author
  • Chen, Chun-Lin
  • Iijima, Miho
ORCID
Venue
Science Signaling
Publisher
American Association for the Advancement of Science (AAAS)
Published
2012-01-31
Volume
5
Issue
209
Pages
ra10-ra10
ISSN
  • 1937-9145 (ISSN-L)
  • 1945-0877
DOI
10.1126/scisignal.2002446
PMC
PMC3381520
OpenAlex
W2073305879
Cited by
70
References
0
Citations by year
2025: 3 · 2023: 1 · 2022: 2 · 2021: 8 · 2020: 5 · 2019: 10 · 2018: 2 · 2017: 3 · 2016: 7 · 2015: 5 · 2014: 9 · 2013: 12 · 2012: 3
FWCI
3.73
Type
journal article
Language
en
Open access
Locations
  • Science Signaling (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of General Medical Sciences (GM-084015, R01GM089853, GM089853, R01GM084015)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
myosin I, phosphatidylinositol 3,4,5-trisphosphate, PIP3 signaling, actin cytoskeleton remodeling, chemotaxis, Dictyostelium, membrane recruitment, actin polymerization, neutrophils, phosphatidylinositol 4,5-bisphosphate
MeSH terms
Cell Line, Cell Membrane, Chemotaxis, Dictyostelium, Humans, Actin Cytoskeleton, Neutrophils, Signal Transduction, Protozoan Proteins, Protein Structure, Tertiary, Phosphatidylinositol Phosphates, HL-60 Cells, Phosphatidylinositol 4,5-Diphosphate, Myosin Type I

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