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ARF proteins: roles in membrane traffic and beyond
TLDR
The understanding of the signalling pathways that are regulated by ARF1 and ARF6, two of the best characterized ARF proteins, provide a molecular context for ARF protein function in fundamental biological processes, such as secretion, endocytosis, phagocyTosis, cytokinesis, cell adhesion and tumour-cell invasion.
Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia
TLDR
Current knowledge about MT1-MMP trafficking and its importance for the regulation of protease activity at invadopodia is reviewed and new insight is brought into mechanisms of cancer-cell invasion and reveals potential pharmacological targets.
Segment-specific expression of a zinc-finger gene in the developing nervous system of the mouse
TLDR
The demonstration that neuromeres are domains of gene expression provides molecular evidence for the segmentation of the CNS.
Collective migration of an epithelial monolayer in response to a model wound
TLDR
Dealing with Madin–Darby canine kidney cells on various surfaces, it is found that a sudden release of the available surface is sufficient to trigger collective motility, which is characterized by a duality between collective and individual behaviors.
The interaction of IQGAP1 with the exocyst complex is required for tumor cell invasion downstream of Cdc42 and RhoA
TLDR
It is proposed that invadopodia function in tumor cells relies on the coordination of cytoskeletal assembly and exocytosis downstream of Rho guanosine triphosphatases.
EFA6, a sec7 domain‐containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization
TLDR
It is demonstrated that by catalyzing nucleotide exchange on ARF6 at the plasma membrane and by regulating Rac1 activation, EFA6 coordinates endocytosis with cytoskeletal rearrangements and promotes the redistribution of transferrin receptors to the cell surface.
Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics
TLDR
A role is established for ARHGAP10 — a novel Rho GTPase-activating protein (Rho-GAP) that is recruited to Golgi membranes through binding to GTP-ARF1 and regulates the Arp2/3 complex and F-actin dynamics at the Golgi through the control of Cdc42 activity.
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