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    In a budding yeast cell overexpressing the nuclear membrane protein Kar1, the spindle pole body bridge—a structure that promotes the organelle’s duplication—is abnormally extended. Seybold et al. reveal that Kar1 anchors the bridge to the nuclear envelope and, together with Cdc31, stabilizes its other cytoplasmic component, Sfi1.
    Image © 2015 Seybold et al.
    See page 843.

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ISSN 0021-9525
EISSN 1540-8140
In this Issue

In Focus

Study reveals that turnover of lamellipodial actin networks helps fibroblasts follow adhesive guidance cues.

In This Issue

People & Ideas

Gracheva studies the molecular basis and evolutionary origins of hibernation.

From the Archive

In 1990, John Pringle and colleagues identified the small GTPase and demonstrated its role in yeast cell polarization.

Review

Report

Studying CENP-A nucleosome assembly in a cell-free system defines the role of existing CENP-A nucleosomes in centromere maintenance.

The primary activity of GMFβ in vivo is actin branch disassembly (and not inhibition of Arp2/3 activation), and this activity plays an important role in lamellipodial dynamics and directional migration toward ECM cues.

Article

Both N- and C-terminal microtubule (MT)-binding domains of CENP-F can follow depolymerizing MT ends while bearing a significant load, and the N-terminal domain prefers binding to curled oligomers of tubulin relative to MT walls by approximately fivefold, suggesting that CENP-F may play a role in the firm bonds that form between kinetochores and the flared plus ends of dynamic MTs.

In response to mating pheromone, the yeast MFA2 mRNA is transported to the tip of the mating projection as an RNP granule and translated; integrity of the granules is required for normal mRNA transport and for the mating process.

Kar1 interacts with the C-terminal (CT) region of Sfi1 to tether the yeast centrosome’s bridge to the nuclear envelope; Sfi1-CT and C-terminal Cdc31-binding regions form the antiparallel Sfi1 overlap in the bridge.

Binding of STIL activates Plk4, and the subsequent phosphorylation of STIL by Plk4 primes the binding of STIL to SAS6 to promote centriole assembly.

P2X4 and calmodulin form a signaling complex in late endosomes and lysosomes that promotes fusion and vacuolation in a Ca2+-dependent fashion.

Tools

A novel method called kinase-interacting substrate screening based on affinity beads coated with the kinase of interest identifies phosphorylation sites for Rho-kinase and others, which reveals that Rho-kinase substrate Scrib plays a crucial role in the regulation of subcellular contractility by assembling with Rho-kinase and Shroom2.

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