A Hydrodynamic Instability Drives Protein Droplet Formation on Microtubules to Nucleate Branches

نویسندگان

چکیده

Liquid-liquid phase separation occurs not only in bulk liquid, but also on surfaces. In physiology, the nature and function of condensates cellular structures is just beginning to be explored. Here, we study how condensed protein TPX2 behaves microtubules initiate branching microtubule nucleation, process by which nucleate off sides preexisting microtubules. This autocatalytic nucleation pathway critical for spindle assembly eukaryotic cells. Using fluorescence, electron, atomic force microscopies hydrodynamic theory, show that a reorganizes according Rayleigh-Plateau instability. same phenomenon causes film dew form droplets along spider web. After uniformly coating microtubules, forms regularly spaced from branches nucleate. Droplet size spacing increase with greater concentration. A stochastic model shows make more efficient confining space where multiple necessary factors colocalize branch. Our work first demonstration instability nanoscale molecular biology. Although it context generic requires coat filament. Thus, anticipate similar effects may play important roles other areas wherever proteins biological filaments meet.

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

-tubulin Complexes that Differ in Their Ability to Nucleate Microtubules

g -tubulin exists in two related complexes in Drosophila embryo extracts (Moritz, M., Y. Zheng, B.M. Alberts, and K. Oegema. 1998. J. Cell Biol. 142:1– 12). Here, we report the purification and characterization of both complexes that we name g -tubulin small complex ( g TuSC; z 280,000 D) and Drosophila g TuRC ( z 2,200,000 D). In addition to g -tubulin, the g TuSC contains Dgrip84 and Dgrip91,...

متن کامل

Protein Folding Drives Disulfide Formation

PDI catalyzes the oxidative folding of disulfide-containing proteins. However, the sequence of reactions leading to a natively folded and oxidized protein remains unknown. Here we demonstrate a technique that enables independent measurements of disulfide formation and protein folding. We find that non-native disulfides are formed early in the folding pathway and can trigger misfolding. In contr...

متن کامل

Note on the dynamic instability of microtubules

Note on the dynamic instability of microtubules Abstract If the dynamic instability of microtubules follows a gamma distribution then one can associate to it a Cantor set. Microtubules (MTs), the main protein polymeric filaments of the cell cy-toskeleton, are a well-defined biological system where methods in condensed matter, statistical mechanics and the theory of complex systems have been app...

متن کامل

Characterization of Two Related Drosophila γ-tubulin Complexes that Differ in Their Ability to Nucleate Microtubules

gamma-tubulin exists in two related complexes in Drosophila embryo extracts (Moritz, M., Y. Zheng, B.M. Alberts, and K. Oegema. 1998. J. Cell Biol. 142:1- 12). Here, we report the purification and characterization of both complexes that we name gamma-tubulin small complex (gammaTuSC; approximately 280,000 D) and Drosophila gammaTuRC ( approximately 2,200,000 D). In addition to gamma-tubulin, th...

متن کامل

Basic Fibroblast Growth Factor Elicits Formation of Interstitial Axonal Branches via Enhanced Severing of Microtubules

The formation of interstitial axonal branches involves the severing of microtubules at sites where new branches form. Here we wished to ascertain whether basic fibroblast growth factor (bFGF) enhances axonal branching through alterations in proteins involved in the severing of microtubules. We found that treatment of cultured hippocampal neurons with bFGF heightens expression of both katanin an...

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: Biophysical Journal

سال: 2021

ISSN: ['0006-3495', '1542-0086']

DOI: https://doi.org/10.1016/j.bpj.2020.11.1452