Rapid Assembly of a Polar Network Architecture Drives Efficient Actomyosin Contractility

نویسندگان

چکیده

Actin network architecture and dynamics play a central role in cell contractility tissue morphogenesis. Pulsed contractions driven by RhoA represent generic mode of actomyosin contractility, but the mechanisms underlying (1) how their specific emerges, (2) this supports contractile function network, remain unclear. Here, we combine quantitative microscopy, single-molecule imaging, numerical simulations simple mathematical modelling, to explore dynamic pulsed contraction. We show that during contractions, two subpopulations formins are recruited from cytoplasm bind surface early C. elegans embryo: formins, functionally inactive population, elongating which actively participate actin filaments elongation. Focusing on formin pulses, minority precede kinetic compatible with capturing rapidly saturating barbed ends available for filament then these assemble polar actin, pointing out pulse, rather than mechanical control architecture. Finally, our demonstrate geometry favors rapid Our results thus saturate convert local, biochemical gradient activity into architecture, thereby driving efficient an important evolutionary feature metazoan embryonic cycles.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Active contractility in actomyosin networks.

Contractile forces are essential for many developmental processes involving cell shape change and tissue deformation. Recent experiments on reconstituted actomyosin networks, the major component of the contractile machinery, have shown that active contractility occurs above a threshold motor concentration and within a window of cross-link concentration. We present a microscopic dynamic model th...

متن کامل

An EMMPRIN-γ-catenin-Nm23 complex drives ATP production and actomyosin contractility at endothelial junctions.

Cell-cell adhesions are important sites through which cells experience and resist forces. In endothelial cells, these forces regulate junction dynamics and determine endothelial barrier strength. We identify the Ig superfamily member EMMPRIN (also known as basigin) as a coordinator of forces at endothelial junctions. EMMPRIN localization at junctions correlates with endothelial junction strengt...

متن کامل

Architecture and Connectivity Govern Actin Network Contractility

Actomyosin contractility plays a central role in a wide range of cellular processes, including the establishment of cell polarity, cell migration, tissue integrity, and morphogenesis during development. The contractile response is variable and depends on actomyosin network architecture and biochemical composition. To determine how this coupling regulates actomyosin-driven contraction, we used a...

متن کامل

Assembly and positioning of actomyosin rings by contractility and planar cell polarity

The actomyosin cytoskeleton is a primary force-generating mechanism in morphogenesis, thus a robust spatial control of cytoskeletal positioning is essential. In this report, we demonstrate that actomyosin contractility and planar cell polarity (PCP) interact in post-mitotic Ciona notochord cells to self-assemble and reposition actomyosin rings, which play an essential role for cell elongation. ...

متن کامل

Actomyosin contractility rotates the cell nucleus

The cell nucleus functions amidst active cytoskeletal filaments, but its response to their contractile stresses is largely unexplored. We study the dynamics of the nuclei of single fibroblasts, with cell migration suppressed by plating onto micro-fabricated patterns. We find the nucleus undergoes noisy but coherent rotational motion. We account for this observation through a hydrodynamic approa...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Social Science Research Network

سال: 2021

ISSN: ['1556-5068']

DOI: https://doi.org/10.2139/ssrn.3780278