The actin module of endocytic internalization in Aspergillus nidulans: A critical role of the WISH/DIP/SPIN90 family protein Dip1.

ABSTRACT: Using fluorescent protein-tagged F-actin reporters we studied the actin cytoskeleton in Aspergillus nidulans. F-actin probes labeled endocytic patches, contractile actin rings and the Spitzenkörper (SPK), but not exocytic cables generated by the SPK-associated formin, illuminated only by tropomyosin. The SPK actin mesh contains tropomyosin and capping protein, but not fimbrin or Arp2/3, showing that it does not involve branched actin. Arp2/3 and fimbrin are recruited to endocytic patches at the end of their lifecycle, staying in them for 12-14 sec, coinciding with the burst of branched actin polymerization that powers vesicle internalization, whereas verprolin stays only during the first half of this actin phase. Hyphal growth requires endocytic recycling, which we exploited to assess the

SUBMITTER: Delgado M 

PROVIDER: S-EPMC12422587 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature