ArticleMolecular biology of the cell2020
Arl4D-EB1 interaction promotes centrosomal recruitment of EB1 and microtubule growth.
Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- TBC1D15 functions as an Arl4D GAP and promotes the mitochondrial translocation of Arl4D for organelle homeostasis.Journal of cell science · 2026Article
- Intervention of machine learning in bladder cancer research using multi-omics datasets: systematic review on biomarker identification.Discover oncology · 2025Review
- Small GTPase ARL4C Associated with Various Cancers Affects Microtubule Nucleation.Biomedicines · 2024Article
- Exploring novel drug targets for erectile dysfunction through plasma proteome with genome.Sexual medicine · 2024Article
- Mapping the global interactome of the ARF family reveals spatial organization in cellular signaling pathways.Journal of cell science · 2024Article
- Identification of mBMC medical genomics · 2023Article
- The ADP-Ribosylation Factor 4d Restricts Regulatory T-Cell Induction via Control of IL-2 Availability.Cells · 2022Article
- Identification and validation of seven RNA binding protein genes as a prognostic signature in oral cavity squamous cell carcinoma.Bioengineered · 2021Article
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADP-ribosylation factor (Arf)-like 4D (Arl4D), one of the Arf-like small GTPases, functions in the regulation of cell morphology, cell migration, and actin cytoskeleton remodeling. End-binding 1 (EB1) is a microtubule (MT) plus-end tracking protein that preferentially localizes at the tips of the plus ends of growing MTs and at the centrosome. EB1 depletion results in many centrosome-related defects. Here, we report that Arl4D promotes the recruitment of EB1 to the centrosome and regulates MT nucleation. We first showed that Arl4D interacts with EB1 in a GTP-dependent manner. This interaction is dependent on the C-terminal EB homology region of EB1 and partially dependent on an SxLP motif of Arl4D. We found that Arl4D colocalized with γ-tubulin in centrosomes and the depletion of Arl4D resulted in a centrosomal MT nucleation defect. We further demonstrated that abolishing Arl4D-EB1 interaction decreased MT nucleation rate and diminished the centrosomal recruitment of EB1 without affecting MT growth rate. In addition, Arl4D binding to EB1 increased the association between the p150 subunit of dynactin and the EB1, which is important for MT stabilization. Together, our results indicate that Arl4D modulates MT nucleation through regulation of the EB1-p150 association at the centrosome.
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