Results 71 to 80 of about 976,237 (341)

Synergy between Wsp1 and Dip1 may initiate assembly of endocytic actin networks

open access: yeseLife, 2020
The actin filament nucleator Arp2/3 complex is activated at cortical sites in Schizosaccharomyces pombe to assemble branched actin networks that drive endocytosis.
Connor J Balzer   +5 more
doaj   +1 more source

Dynamic actin cycling through mitochondrial subpopulations locally regulates the fission–fusion balance within mitochondrial networks

open access: yesNature Communications, 2016
Mitochondria form interconnected networks that dynamically remodel in response to cellular needs. Using live-cell imaging, we investigate the role of the actin cytoskeleton in regulating mitochondrial fission and fusion.
Andrew S. Moore   +3 more
semanticscholar   +1 more source

Rewriting the dendritic cell code in cancer—from subset identity to immunotherapeutic design

open access: yesFEBS Letters, EarlyView.
Dendritic cells (DCs) play central roles in cancer immunity but are often subverted by the tumor microenvironment. This review explores the diversity of DC subsets, their functional plasticity, and emerging therapeutic strategies to reprogram DCs for enhanced antitumor responses, including vaccines, in vivo targeting, and DC‐based immunotherapies ...
Estevão Carlos Silva Barcelos   +3 more
wiley   +1 more source

Dynamic recruitment of the curvature-sensitive protein ArhGAP44 to nanoscale membrane deformations limits exploratory filopodia initiation in neurons

open access: yeseLife, 2014
In the vertebrate central nervous system, exploratory filopodia transiently form on dendritic branches to sample the neuronal environment and initiate new trans-neuronal contacts.
Milos Galic   +5 more
doaj   +1 more source

Molecular basis for substrate specificity of the Phactr1/PP1 phosphatase holoenzyme

open access: yeseLife, 2020
PPP-family phosphatases such as PP1 have little intrinsic specificity. Cofactors can target PP1 to substrates or subcellular locations, but it remains unclear how they might confer sequence-specificity on PP1.
Roman O Fedoryshchak   +10 more
doaj   +1 more source

TOMM20 as a driver of cancer aggressiveness via oxidative phosphorylation, maintenance of a reduced state, and resistance to apoptosis

open access: yesMolecular Oncology, EarlyView.
TOMM20 increases cancer aggressiveness by maintaining a reduced state with increased NADH and NADPH levels, oxidative phosphorylation (OXPHOS), and apoptosis resistance while reducing reactive oxygen species (ROS) levels. Conversely, CRISPR‐Cas9 knockdown of TOMM20 alters these cancer‐aggressive traits.
Ranakul Islam   +9 more
wiley   +1 more source

A novel mode of capping protein-regulation by twinfilin

open access: yeseLife, 2018
Cellular actin assembly is controlled at the barbed ends of actin filaments, where capping protein (CP) limits polymerization. Twinfilin is a conserved in vivo binding partner of CP, yet the significance of this interaction has remained a mystery.
Adam B Johnston   +8 more
doaj   +1 more source

The atypical KRASQ22K mutation directs TGF‐β response towards partial epithelial‐to‐mesenchymal transition in patient‐derived colorectal cancer tumoroids

open access: yesMolecular Oncology, EarlyView.
TGF‐β has a complex role in cancer, exhibiting both tumor‐suppressive and tumor‐promoting properties. Using a series of differentiated tumoroids, derived from different stages and mutational background of colorectal cancer patients, we replicate this duality of TGF‐β in vitro. Notably, the atypical but highly aggressive KRASQ22K mutation rendered early‐
Theresia Mair   +17 more
wiley   +1 more source

It takes two

open access: yeseLife, 2015
Two forms of an unconventional myosin motor protein have separate functions in the growth and maintenance of hair bundles in auditory hair cells.
Teresa Nicolson
doaj   +1 more source

The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments.

open access: yesProceedings of the National Academy of Sciences of the United States of America, 1998
The Arp2/3 complex is a stable assembly of seven protein subunits including two actin-related proteins (Arp2 and Arp3) and five novel proteins. Previous work showed that this complex binds to the sides of actin filaments and is concentrated at the ...
R. Mullins, Heuser Ja, T. Pollard
semanticscholar   +1 more source

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