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In Focus

When cells let go of a surface, they don't let go of their integrins.

People & Ideas

Melchior's laboratory is exploring the regulation and consequences of protein modification by the small protein SUMO.



The BubR1 kinase domain controls spindle attachment to the kinetochores, whereas the KEN domain regulates activation of the spindle assembly checkpoint.

Cohesin subunit Scc1 and Akt kinase–interacting protein 1 both localize to centrosomes and regulate the timing of centriole separation during mitosis.

KIF9B localizes to the axoneme and basal body and is needed for flagella assembly, whereas KIF9A localizes only to the axoneme and controls flagella motility without affecting their structure.


Experimental attempts to activate replication origins within the temporal transition region in the IgH locus in mouse embryonic stem cells were not successful, and thus, why and how they become activated in B cells remains unclear.

INCENP fine tunes the level of aurora B kinase activity, which in turn correlates with different functional states of the chromosome passenger complex.

An E2–E3 complex can ubiquitinate substrates via either an isopeptide bond (to a lysine) or an ester bond (to a serine or threonine) and preferentially uses the latter to induce ERAD.

The PRELP heparin sulfate–binding protein translocates to the nucleus, where it impairs NF-κB transcriptional activity, which in turn regulates bone homeostasis.

Hedgehog protein IHH expression is regulated by transcription factor δ-EF1 to control endochondral bone formation

In Special Collection: JCB65: Lipid and Membrane Biology

PIP5K is held at the membrane of forming phagosomes by a conserved, positively charged patch. During particle engulfment, the surface charge of the phagosome decreases, releasing PIP5K and enabling phagocytosis to proceed.

A talin intermolecular interaction autoinhibits its own activation and regulates β3-integrin binding. When bound, β3-integrin undergoes structural alterations that prevent its β and α subunits from associating, maintaining β3-integrin's clustering capability.

A new mechanism for focal adhesion disassembly is described involving microtubule-stimulated endocytosis of integrins at focal adhesions.


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