@article{14846, abstract = {Contraction and flow of the actin cell cortex have emerged as a common principle by which cells reorganize their cytoplasm and take shape. However, how these cortical flows interact with adjacent cytoplasmic components, changing their form and localization, and how this affects cytoplasmic organization and cell shape remains unclear. Here we show that in ascidian oocytes, the cooperative activities of cortical actomyosin flows and deformation of the adjacent mitochondria-rich myoplasm drive oocyte cytoplasmic reorganization and shape changes following fertilization. We show that vegetal-directed cortical actomyosin flows, established upon oocyte fertilization, lead to both the accumulation of cortical actin at the vegetal pole of the zygote and compression and local buckling of the adjacent elastic solid-like myoplasm layer due to friction forces generated at their interface. Once cortical flows have ceased, the multiple myoplasm buckles resolve into one larger buckle, which again drives the formation of the contraction pole—a protuberance of the zygote’s vegetal pole where maternal mRNAs accumulate. Thus, our findings reveal a mechanism where cortical actomyosin network flows determine cytoplasmic reorganization and cell shape by deforming adjacent cytoplasmic components through friction forces.}, author = {Caballero Mancebo, Silvia and Shinde, Rushikesh and Bolger-Munro, Madison and Peruzzo, Matilda and Szep, Gregory and Steccari, Irene and Labrousse Arias, David and Zheden, Vanessa and Merrin, Jack and Callan-Jones, Andrew and Voituriez, Raphaël and Heisenberg, Carl-Philipp J}, issn = {1745-2481}, journal = {Nature Physics}, publisher = {Springer Nature}, title = {{Friction forces determine cytoplasmic reorganization and shape changes of ascidian oocytes upon fertilization}}, doi = {10.1038/s41567-023-02302-1}, year = {2024}, } @article{9379, abstract = {When B cells encounter membrane-bound antigens, the formation and coalescence of B cell antigen receptor (BCR) microclusters amplifies BCR signaling. The ability of B cells to probe the surface of antigen-presenting cells (APCs) and respond to APC-bound antigens requires remodeling of the actin cytoskeleton. Initial BCR signaling stimulates actin-related protein (Arp) 2/3 complex-dependent actin polymerization, which drives B cell spreading as well as the centripetal movement and coalescence of BCR microclusters at the B cell-APC synapse. Sustained actin polymerization depends on concomitant actin filament depolymerization, which enables the recycling of actin monomers and Arp2/3 complexes. Cofilin-mediated severing of actin filaments is a rate-limiting step in the morphological changes that occur during immune synapse formation. Hence, regulators of cofilin activity such as WD repeat-containing protein 1 (Wdr1), LIM domain kinase (LIMK), and coactosin-like 1 (Cotl1) may also be essential for actin-dependent processes in B cells. Wdr1 enhances cofilin-mediated actin disassembly. Conversely, Cotl1 competes with cofilin for binding to actin and LIMK phosphorylates cofilin and prevents it from binding to actin filaments. We now show that Wdr1 and LIMK have distinct roles in BCR-induced assembly of the peripheral actin structures that drive B cell spreading, and that cofilin, Wdr1, and LIMK all contribute to the actin-dependent amplification of BCR signaling at the immune synapse. Depleting Cotl1 had no effect on these processes. Thus, the Wdr1-LIMK-cofilin axis is critical for BCR-induced actin remodeling and for B cell responses to APC-bound antigens.}, author = {Bolger-Munro, Madison and Choi, Kate and Cheung, Faith and Liu, Yi Tian and Dang-Lawson, May and Deretic, Nikola and Keane, Connor and Gold, Michael R.}, issn = {2296-634X}, journal = {Frontiers in Cell and Developmental Biology}, keywords = {B cell, actin, immune synapse, cell spreading, cofilin, WDR1 (AIP1), LIM domain kinase, B cell receptor (BCR)}, publisher = {Frontiers Media}, title = {{The Wdr1-LIMK-Cofilin axis controls B cell antigen receptor-induced actin remodeling and signaling at the immune synapse}}, doi = {10.3389/fcell.2021.649433}, volume = {9}, year = {2021}, }