ArticleMolecular biology of the cell2002
PLAC-24 is a cytoplasmic dynein-binding protein that is recruited to sites of cell-cell contact.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Intrinsic disorder in dynein intermediate chain modulates its interactions with NudE and dynactin.The Journal of biological chemistry · 2012Article
- Article
- Recruitment of dynein to late endosomes and lysosomes through light intermediate chains.Molecular biology of the cell · 2011Article
- Light chain-dependent self-association of dynein intermediate chain.The Journal of biological chemistry · 2011Article
- Adherens junctions: from molecules to morphogenesis.Nature reviews. Molecular cell biology · 2010Review
- Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Recruitment of dynein to the Jurkat immunological synapse.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Human enhancer of invasion-cluster, a coiled-coil protein required for passage through mitosis.Molecular and cellular biology · 2004Article
- Neuronal migration illuminated: a look under the hood of the living neuron.Cell adhesion & migrationArticle
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
We screened for polypeptides that interact specifically with dynein and identified a novel 24-kDa protein (PLAC-24) that binds directly to dynein intermediate chain (DIC). PLAC-24 is not a dynactin subunit, and the binding of PLAC-24 to the dynein intermediate chain is independent of the association between dynein and dynactin. Immunocytochemistry using PLAC-24-specific polyclonal antibodies revealed a punctate perinuclear distribution of the polypeptide in fibroblasts and isolated epithelial cells. However, as epithelial cells in culture make contact with adjacent cells, PLAC-24 is specifically recruited to the cortex at sites of contact, where the protein colocalizes with components of the adherens junction. Disruption of the cellular cytoskeleton with latrunculin or nocodazole indicates that the localization of PLAC-24 to the cortex is dependent on intact actin filaments but not on microtubules. Overexpression of beta-catenin also leads to a loss of PLAC-24 from sites of cell-cell contact. On the basis of these data and the recent observation that cytoplasmic dynein is also localized to sites of cell-cell contact in epithelial cells, we propose that PLAC-24 is part of a multiprotein complex localized to sites of intercellular contact that may function to tether microtubule plus ends to the actin-rich cellular cortex.
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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.