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In Focus

The small GTPase forms an organized scaffold that can regulate the pinching of vesicles from the ER.

People & Ideas

David Pellman investigates the constraints and advantages that alteration of chromosome number places on dividing cells.



Review series


To satisfy the mitotic checkpoint and drive chromosome congression, the Mps1 kinase lets go of kinetochores by phosphorylating itself in trans (see also related papers by Maciejowski et al. and Santaguida et al. in this issue).

Depletion of MCAK, which lengthens astral microtubules, induces oscillations of the mitotic spindle, and displaces the plane of cell division.

The PAFAH 1b complex links phospholipid remodeling and membrane tubulation within the Golgi to dynein-dependent transport.

Whittling away SNARE complex components reveals essential domains for Munc18-1–mediated membrane fusion.

Mot48, a PIH domain protein, assembles and stabilizes inner arm dynein complexes in the cytoplasm before they are transported into cilia.


Addition of reversine to dividing cells ejects Mad1 and the RZZ complex from unattached kinetochores and prevents resolution of incorrect chromosome–microtubule attachments (see also related papers by Hewitt et al. and Maciejowski et al. in this issue).

Cdc20 and Mad2 or Bub1 don’t come together in Mps1-null cells, resulting in a dramatic acceleration of anaphase onset (see also related papers by Hewitt et al. and Santaguida et al. in this issue).

In addition to its function as an Arp2/3 complex subunit, Arp1cb interacts with and stimulates Aurora A at centrosomes, functioning in cell cycle progression.

While dynamin pinches vesicles from the plasma membrane, the Sar1 GTPase specializes in cinching ER membrane tubules.

Macrophages lacking SPSB2 have increased NO production and enhanced pathogen-killing capabilities due to decreased ubiquitin-mediated destruction of iNOS.

The Chlamydia-encoded protein Tarp is phosphorylated in the host cell cytoplasm and is a multivalent hub for antiapoptotic signaling molecules.

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