Skip to Main Content

Advertisement

Issues

  • Cover Image

    Cover Image

    issue cover

    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.
    See page 889.

  • PDF Icon PDF LinkTable of Contents
  • PDF Icon PDF LinkEditorial Board
ISSN 0021-9525
EISSN 1540-8140
In this Issue

In This Issue

In Focus

Proteins combine into filaments that hug and modify the membrane.

People & Ideas

Since discovering ankyrin, Bennett has worked to understand its many functions at cell membranes.

Review

Report

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.

FAK promotes the epithelial–mesenchymal transition in mouse embryonic cells by regulating the transcription factor Snail1.

Article

Replication forks stalled by excess DNA supercoiling can be resolved by DNA cleavage by the Mus81 endonuclease.

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.

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.

CK1delta binds and phosphorylates the microtubule plus-end–binding protein EB1 and promotes centrosome translocation to the immunological synapse in T cells.

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.

Mammalian SEPT9 is positioned at the end of septin octamers and is necessary for octamer assembly into polymers necessary for abscission during cytokinesis.

In the absence of Crumbs, myosin V is degraded, resulting in defective rhodopsin 1 transport to the rhabdomere and subsequent photoreceptor degeneration.

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.

A Rac–PAK1–Ajuba feedback loop stabilizes cadherin complexes via coordination of spatiotemporal signaling with actin remodeling at cell–cell contacts.

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.

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 induces recruitment of the sodium-hydrogen exchanger NHE1 to invadopodia, resulting in pH changes that regulate cortactin-cofilin binding and invadopodium dynamics.

Close Modal
This Feature Is Available To Subscribers Only

Sign In or Create an Account

Close Modal
Close Modal