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    As depicted in this 3D reconstruction of a Tetrahymena thermophila cell, secretory granules known as mucocysts (green) move through the cytoplasm to dock at the plasma membrane. Colored lines show the trajectories of the mobile mucocyst pool. Briguglio et al. reveal that the sortilin family of lysosomal sorting receptors deliver non-aggregated cargo proteins to the granules.
    Image © 2013 Briguglio et al., and prepared with the help of Christine Labno.
    See page 537.

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ISSN 0021-9525
EISSN 1540-8140
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In This Issue

In Focus

Lysosomal sorting receptors transport cargo to secretory granules in Tetrahymena.

People & Ideas

Bakal studies the signaling networks that control cell shape.


Cell biology in neuroscience


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Septin-dependent removal of membrane-associated Anillin and Sticky-dependent retention of Anillin are required for contractile ring stability and closure and for midbody ring formation.

The septins, but not midbody microtubules, are important for daughter cell cytoplasmic isolation and ESCRT-dependent midbody ring release during abscission.

Synaptic stimulation promotes proteasome-dependent degradation of p35, inactivation of Cdk5, and decreased phosphorylation of PP1, allowing PP1 to act in the induction of long-term depression.

The delivery of nonaggregated cargo proteins to Tetrahymena secretory granules requires receptors of the sortilin/VPS10 family, proteins classically associated with lysosome biogenesis.

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