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Cover Image
Cover Image
On the cover
An electron micrograph of the cytoplasmic face of a budding yeast’s plasma membrane shows a filamentous structure formed by eisosome proteins (immunolabeled with gold particles) next to a membrane invagination. Karotki et al. reveal that eisosome components spatially organize the plasma membrane by assembling into a lipid-binding scaffold. Image courtesy of Lena Karotki.
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In This Issue
In Focus
How eisosomes help the plasma membrane get organized
Proteins combine into filaments that hug and modify the membrane.
People & Ideas
Vann Bennett: How ankyrin holds it all together
Since discovering ankyrin, Bennett has worked to understand its many functions at cell membranes.
Review
Report
Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament
In vitro, actin filament tension correlates with the binding and apparent activity of the filament-severing protein cofilin, suggesting a molecular mechanism by which cells respond to changes in mechanical force.
Snail1 controls epithelial–mesenchymal lineage commitment in focal adhesion kinase–null embryonic cells
FAK promotes the epithelial–mesenchymal transition in mouse embryonic cells by regulating the transcription factor Snail1.
Article
Mus81-mediated DNA cleavage resolves replication forks stalled by topoisomerase I–DNA complexes
Replication forks stalled by excess DNA supercoiling can be resolved by DNA cleavage by the Mus81 endonuclease.
Identification of host cell factors required for intoxication through use of modified cholera toxin
A novel labeling strategy is applied to cholera toxin subunit A1 in the context of a pre-assembled holotoxin allowing tracking of its intracellular trafficking pathway and identification of host proteins involved in cell intoxication.
VPS35 haploinsufficiency increases Alzheimer’s disease neuropathology
The retromer complex component VPS35 prevents activation of the BACE1 and Aβ production and thus plays an essential role in limiting Alzheimer’s disease neuropathology.
Casein kinase I delta controls centrosome positioning during T cell activation
CK1delta binds and phosphorylates the microtubule plus-end–binding protein EB1 and promotes centrosome translocation to the immunological synapse in T cells.
Myosin concentration underlies cell size–dependent scalability of actomyosin ring constriction
The rate of actomyosin ring constriction in cells of different sizes correlates with myosin motor concentration in Neurospora crassa cells, leading to increased division rates in larger cells during cytokinesis.
SEPT9 occupies the terminal positions in septin octamers and mediates polymerization-dependent functions in abscission
Mammalian SEPT9 is positioned at the end of septin octamers and is necessary for octamer assembly into polymers necessary for abscission during cytokinesis.
Crumbs regulates rhodopsin transport by interacting with and stabilizing myosin V
In the absence of Crumbs, myosin V is degraded, resulting in defective rhodopsin 1 transport to the rhabdomere and subsequent photoreceptor degeneration.
Release of serine/threonine-phosphorylated adaptors from signaling microclusters down-regulates T cell activation
Serine/threonine phosphorylation of the T cell adaptor proteins SLP76 and GADS by HPK1 induces their release from signaling microclusters and subsequent termination of the T cell response.
Ajuba is required for Rac activation and maintenance of E-cadherin adhesion
A Rac–PAK1–Ajuba feedback loop stabilizes cadherin complexes via coordination of spatiotemporal signaling with actin remodeling at cell–cell contacts.
E–N-cadherin heterodimers define novel adherens junctions connecting endoderm-derived cells
Contradicting the “cadherin switch” model, mixed E-cadherin–N-cadherin heterodimeric adherens junctions are prevalent in a variety of endodermal cells and endoderm-derived tumors.
Eisosome proteins assemble into a membrane scaffold
Membrane organization by eisosomes is mediated by self-assembly of its main components into a membrane-bound protein scaffold with lipid-binding specificity.
Cortactin phosphorylation regulates cell invasion through a pH-dependent pathway
Cortactin phosphorylation induces recruitment of the sodium-hydrogen exchanger NHE1 to invadopodia, resulting in pH changes that regulate cortactin-cofilin binding and invadopodium dynamics.
