Unlabelled: Ascochyta blight disease is a devastating disease caused by the fungal pathogen that threatens chickpea production around the globe. Endocytic mechanism has a significant role in fungal growth and virulence. The underlying biology of biogenesis of central component of endocytosis viz Rab5 vesicles, is not completely understood. The involvement of F-BAR domain containing protein (ArF-BAR) in various cellular processes that collectively make ArF-BAR as an important virulence determinant. Here, we report that ArF-BAR is involved in biogenesis and motility of early endosome. In the absence of gene (Δ), fungal mutants exhibited reduced number of EGFP coated ArRab5 vesicles, along with the considerable reduction in their dynamics. Here, we show that ArF-BAR interacts with clathrin light chain (ArCLC), specifically with its F-BAR domain. These findings suggests the novel role of ArF-BAR in biogenesis and dynamics of early endosome. Additionally, ArF-BAR is involved in clathrin-mediated mechanism of endocytosis which is required for host infection and disease development. Identification of this pathway offers new impending targets for disease intervention in plants.
Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-022-03451-5.
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http://dx.doi.org/10.1007/s13205-022-03451-5 | DOI Listing |
Clin Exp Immunol
November 2024
Division of Immunology, Department of Pediatrics, Hacettepe University Medical School, Ankara, Turkey.
J Biol Chem
December 2024
Université Côte d'Azur, CNRS, INSERM, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France. Electronic address:
Heliyon
July 2024
Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Indore bypass Road, Bhopal 462 066, Madhya Pradesh, India.
Intracellular membrane tubules play a crucial role in diverse cellular processes, and their regulation is facilitated by Bin-Amphiphysin-Rvs (BAR) domain-containing proteins. This study investigates the roles of ICA69 (dICA69) (an N-BAR protein) and CIP4 (dCIP4) (an F-BAR protein), focusing on their impact on membrane tubule organization. In contrast to the prevailing models of BAR-domain protein function, we observed colocalization of endogenous dICA69 with dCIP4-induced tubules, indicating their potential recruitment for tubule formation and maintenance.
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April 2024
CRBM (Centre de Recherche en Biologie cellulaire de Montpellier), University of Montpellier, CNRS UMR 5237, 34293, Montpellier, France.
A double septin ring accompanies cytokinesis in yeasts and mammalian cells. In budding yeast, reorganisation of the septin collar at the bud neck into a dynamic double ring is essential for actomyosin ring constriction and cytokinesis. Septin reorganisation requires the Mitotic Exit Network (MEN), a kinase cascade essential for cytokinesis.
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March 2024
Department of Cell Biology, Yale University School of Medicine, New Haven, CT, United States.
The coordination between actin and microtubule network is crucial, yet this remains a challenging problem to dissect and our understanding of the underlying mechanisms remains limited. In this study, we used travelling waves in the cell cortex to characterize the collective dynamics of cytoskeletal networks. Our findings show that Cdc42 and F-BAR-dependent actin waves in mast cells are mainly driven by formin-mediated actin polymerization, with the microtubule-binding formin FH2 domain-containing protein 1 (FHDC1) as an early regulator.
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