Journal of Cell Biology
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- Gale, Aaas, Proquest, Highwire from 1955, Csh, Jstor, Aacr, Nephrology, Endocrine, The Rockefeller University Press, Rupress, CSA, and Ama
Soluble oligomers are sufficient for transmission of a yeast prion but do not confer phenotype.
We describe an oligomeric species of a yeast prion protein in cells that is sufficient for prion transmission and infectivity. These oligomers differ from the classic prion aggregates in that they are soluble and less resistant to SDS. We found that large, SDS-resistant aggregates were required for...
The vesicular ATPase: a missing link between acidification and exocytosis.
The vesicular adenosine triphosphatase (ATPase) acidifies intracellular compartments, including synaptic vesicles and secretory granules. A controversy about a second function of this ATPase in exocytosis has been fuelled by questions about multiple putative roles of acidification in the exocytic pr...
Cell biology in neuroscience: RNA-based mechanisms underlying axon guidance.
Axon guidance plays a key role in establishing neuronal circuitry. The motile tips of growing axons, the growth cones, navigate by responding directionally to guidance cues that pattern the embryonic neural pathways via receptor-mediated signaling. Evidence in vitro in the last decade supports the n...
Epiblast integrity requires CLASP and Dystroglycan-mediated microtubule anchoring to the basal cortex.
We show that epiblast epithelial status was maintained by anchoring microtubules to the basal cortex via CLIP-associated protein (CLASP), a microtubule plus-end tracking protein, and Dystroglycan, a transmembrane protein that bridges the cytoskeleton and basement membrane (BM). Mesoderm formation re...
An ESCRT-spastin interaction promotes fission of recycling tubules from the endosome.
We show that cells lacking the MT-severing protein spastin had increased tubulation of and defective receptor sorting through endosomal tubular recycling compartments. Spastin required the ability to sever MTs and to interact with ESCRT-III (a complex controlling cargo degradation) proteins to regul...
The synaptobrevin homologue Snc2p recruits the exocyst to secretory vesicles by binding to Sec6p.
We observe a direct interaction between the exocyst subunit Sec6p and the latter half of the SNARE motif of Snc2p. An snc2 mutation that specifically disrupts this interaction led to exocyst mislocalization and a block in exocytosis in vivo without affecting liposome fusion in vitro. Overexpression...
Macrophage-secreted cytokines drive pancreatic acinar-to-ductal metaplasia through NF-κB and MMPs.
We identify the macrophage-secreted inflammatory cytokines RANTES and tumor necrosis factor α (TNF) as mediators of such signaling. Both RANTES and TNF induce ADM through activation of nuclear factor κB and its target genes involved in regulating survival, proliferation, and degradation of extracell...
Lysosome-mediated processing of chromatin in senescence.
We show that an autophagy/lysosomal pathway processes chromatin in senescent cells. In senescent cells, lamin A/C-negative, but strongly γ-H2AX-positive and H3K27me3-positive, cytoplasmic chromatin fragments (CCFs) budded off nuclei, and this was associated with lamin B1 down-regulation and the loss...
Physical limits of cell migration: Control by ECM space and nuclear deformation and tuning by proteolysis and traction force.
We quantitatively identify the limits of cell migration by physical arrest. MMP-independent migration declined as linear function of pore size and with deformation of the nucleus, with arrest reached at 10% of the nuclear cross section (tumor cells, 7 µm(2); T cells, 4 µm(2); neutrophils, 2 µm(2))....
Spatiotemporal control of PopZ localization through cell cycle-coupled multimerization.
We investigate the mechanisms governing the localization of PopZ, a chromosome-anchoring protein whose unipolar to bipolar localization pattern is critical for cell cycle progression in Caulobacter crescentus. We provide evidence that polar localization of PopZ relied on its self-assembly into a hig...