ArticleEukaryotic cell2014
PakD, a putative p21-activated protein kinase in Dictyostelium discoideum, regulates actin.
Article in Eukaryotic cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Two endogenousProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cdc42/Rac Interactive Binding Containing Effector Proteins in Unicellular Protozoans With Reference to Human Host: Locks of the Rho Signaling.Frontiers in genetics · 2022Review
- A chemorepellent inhibits local Ras activation to inhibit pseudopod formation to bias cell movement away from the chemorepellent.Molecular biology of the cell · 2022Article
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- UsingFrontiers in cell and developmental biology · 2021Review
- An endogenous chemorepellent directs cell movement by inhibiting pseudopods at one side of cells.Molecular biology of the cell · 2019Article
- Phototransduction and circadian entrainment are the key pathways in the signaling mechanism for the baculovirus induced tree-top disease in the lepidopteran larvae.Scientific reports · 2018Article
- Extracellular polyphosphate signals through Ras and Akt to primeJournal of cell science · 2017Article
- Functional interaction of PkcA and PldB regulate aggregation and development in Dictyostelium discoideum.Cellular signalling · 2017Article
- Article
- Cell signaling during development of Dictyostelium.Developmental biology · 2014Review
- Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Proper regulation of the actin cytoskeleton is essential for cell function and ultimately for survival. Tight control of actin dynamics is required for many cellular processes, including differentiation, proliferation, adhesion, chemotaxis, endocytosis, exocytosis, and multicellular development. Here we describe a putative p21-activated protein kinase, PakD, that regulates the actin cytoskeleton in Dictyostelium discoideum. We found that cells lacking pakD are unable to aggregate and thus unable to develop. Compared to the wild type, cells lacking PakD have decreased membrane extensions, suggesting defective regulation of the actin cytoskeleton. pakD(-) cells show poor chemotaxis toward cyclic AMP (cAMP) but normal chemotaxis toward folate, suggesting that PakD mediates some but not all chemotaxis responses. pakD(-) cells have decreased polarity when placed in a cAMP gradient, indicating that the chemotactic defects of the pakD(-) cells may be due to an impaired cytoskeletal response to cAMP. In addition, while wild-type cells polymerize actin in response to global stimulation by cAMP, pakD(-) cells exhibit F-actin depolymerization under the same conditions. Taken together, the results suggest that PakD is part of a pathway coordinating F-actin organization during development.
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