Arpin is an Arp2/3 inhibitory protein, which decreases the protrusion lifetime and hence directional persistence in the migration of diverse cells. Arpin is activated by the small GTPase Rac, which controls cell protrusion, thus closing a negative feedback loop that renders the protrusion intrinsically unstable. Because of these properties, it was proposed that Arpin might play a role in directed migration, where directional persistence has to be fine-tuned. We report here, however, that Arpin-depleted tumour cells and Arpin knock-out Dictyostelium amoeba display no obvious defect in chemotaxis. These results do not rule out a potential role of Arpin in other systems, but argue against a general role of Arpin in chemotaxis.
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http://dx.doi.org/10.1111/boc.201600064 | DOI Listing |
Adv Sci (Weinh)
January 2025
Department of Critical Care Medicine, Zhujiang Hospital, Southern Medical University, Guangzhou, 510280, China.
Older individuals experience increased susceptibility and mortality to bacterial infections, but the underlying etiology remains unclear. Herein, it is shown that aging-associated reduction of commensal Parabacteroides goldsteinii (P. goldsteinii) in both aged mice and humans critically contributes to worse outcomes of bacterial infection.
View Article and Find Full Text PDFCurr Biol
November 2024
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, MO 63110, USA. Electronic address:
Biol Cell
October 2024
Laboratory of Structural Biology of the Cell (BIOC), UMR7654 CNRS/Ecole polytechnique, Institut Polytechnique de Paris, Palaiseau, France.
Background Information: Arpin, an Arp2/3 inhibitory protein, inhibits lamellipodial protrusions and cell migration. Arpin expression is lost in tumor cells of several cancer types.
Results: Here we analyzed expression levels of Arpin and various markers using Reverse Phase Protein Array (RPPA) in human mammary carcinomas.
bioRxiv
May 2024
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO.
Actin polymerization is often associated with membrane proteins containing capping-protein-interacting (CPI) motifs, such as CARMIL, CD2AP, and WASHCAP/Fam21. CPI motifs bind directly to actin capping protein (CP), and this interaction weakens the binding of CP to barbed ends of actin filaments, lessening the ability of CP to functionally cap those ends. The protein V-1 / myotrophin binds to the F-actin binding site on CP and sterically blocks CP from binding barbed ends.
View Article and Find Full Text PDFCells
February 2024
Institute of Experimental Biomedicine-Chair I, University Hospital Würzburg, 97080 Würzburg, Germany.
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