TFG regulates inner COPII coat recruitment to facilitate anterograde secretory protein transport.

Coat protein complex II (COPII) governs the initial steps of biosynthetic secretory protein transport from the endoplasmic reticulum (ER), facilitating the movement of a wide variety of cargoes. Here, we demonstrate that Trk-fused gene (TFG) regulates the rate at which inner COPII coat proteins are concentrated at ER subdomains. Specifically, in cells lacking TFG, the GTPase-activating protein (GAP) Sec23 accumulates more rapidly at budding sites on the ER as compared with control cells, potentially altering the normal timing of GTP hydrolysis on Sar1.

Nutrient deprivation alters the rate of COPII subunit recruitment at ER subdomains to tune secretory protein transport.

Co-assembly of the multilayered coat protein complex II (COPII) with the Sar1 GTPase at subdomains of the endoplasmic reticulum (ER) enables secretory cargoes to be concentrated efficiently within nascent transport intermediates, which subsequently deliver their contents to ER-Golgi intermediate compartments. Here, we define the spatiotemporal accumulation of native COPII subunits and secretory cargoes at ER subdomains under differing nutrient availability conditions using a combination of CRISPR/Cas9-mediated genome editing and live cell imaging. Our findings demonstrate that the rate of inner COPII coat recruitment serves as a determinant for the pace of cargo export, irrespective of COPII subunit expression levels.

The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER.

Coat protein complex II (COPII) plays an integral role in the packaging of secretory cargoes within membrane-enclosed transport carriers that leave the endoplasmic reticulum (ER) from discrete subdomains. Lipid bilayer remodeling necessary for this process is driven initially by membrane penetration mediated by the Sar1 GTPase and further stabilized by assembly of a multilayered complex of several COPII proteins. However, the relative contributions of these distinct factors to transport carrier formation and protein trafficking remain unclear.

Nutrient deprivation alters the rate of COPII coat assembly to tune secretory protein transport.

Co-assembly of the multilayered coat protein complex II (COPII) with the Sari GTPase at subdomains of the endoplasmic reticulum (ER) enables secretory cargoes to be concentrated efficiently within nascent transport intermediates, which subsequently deliver their contents to ER-Golgi intermediate compartments. Here, we define the spatiotemporal accumulation of native COPII subunits and secretory cargoes at ER subdomains under differing nutrient availability conditions using a combination of CRISPR/Cas9-mediated genome editing and live cell imaging. Our findings demonstrate that the rate of inner COPII coat assembly serves as a determinant for the pace of cargo export, irrespective of COPII subunit expression levels.

Quantifying Total and Out-of-Pocket Costs Associated With Head and Neck Cancer Survivorship.

Importance: Oncologic treatment is costly to the health care system and to individuals, but patients with head and neck cancer (HNC) also have long-term care needs after treatment. Survivors of HNC require specific consideration given their rapidly growing numbers. This subpopulation of cancer survivors often experiences long-term treatment-associated morbidity.

Analysis of academic publishing output among 1634 successful applicants in the 2011-2018 neurosurgery residency match.

Background: Research productivity is a key criterion for applicant selection reported by residency program directors. Research volume reported on neurosurgery residency applications has risen steadily over the past decade.

Objective: Perform retrospective bibliographic searches of successful applicants who matched into U.

Downshifting Yeast Dominance: Cell Physiology and Phospholipid Composition Are Altered With Establishment of the [ ] Prion in .

Establishment of the [ ] prion in reduces both transcriptional expression of the hexose transporter gene and fermentation capacity in high sugar conditions. We evaluated the impact of deletion of the gene on the expression of [ ] prion phenotype in a vineyard isolate, UCD932, and found that changes in fermentation capacity were observable even with complete loss of the Hxt3 transporter, suggesting other cellular functions affecting fermentation rate may be impacted in [ ] strains. In a comparison of isogenic [ ] and [ ] strains, localization of the Pma1 plasma membrane ATPase showed differences in distribution within the membrane.

Growth factor stimulation promotes multivesicular endosome biogenesis by prolonging recruitment of the late-acting ESCRT machinery.

The formation of multivesicular endosomes (MVEs) mediates the turnover of numerous integral membrane proteins and has been implicated in the down-regulation of growth factor signaling, thereby exhibiting properties of a tumor suppressor. The endosomal sorting complex required for transport (ESCRT) machinery plays a key role in MVE biogenesis, enabling cargo selection and intralumenal vesicle (ILV) budding. However, the spatiotemporal pattern of endogenous ESCRT complex assembly and disassembly in mammalian cells remains poorly defined.