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We began analyzing https://link.springer.com/article/10.1007/s00418-016-1527-3, but it redirected us to https://link.springer.com/article/10.1007/s00418-016-1527-3. The analysis below is for the second page.

Title[redir]:
Functional characterisation of the YIPF protein family in mammalian cells | Histochemistry and Cell Biology
Description:
In this study, we carry out a systematic characterisation of the YIPF family of proteins with respect to their subcellular localisation profile, membrane topology and functional effects on the endomembrane system. YIPF proteins primarily localise to the Golgi complex and can be grouped into trans-Golgi-localising YIPFs (YIPF1 and YIPF2) and cis-Golgi-localising YIPFs (YIPF3, YIPF4 and YIPF5), with YIPF6 and YIPF7 showing a broader profile being distributed throughout the Golgi stack. YIPF proteins have a long soluble N-terminal region, which is orientated towards the cytosol, followed by 5 closely stacked transmembrane domains, and a C terminus, orientated towards the lumen of the Golgi. The significance of YIPF proteins for the maintenance of the morphology of the Golgi was tested by RNA interference, revealing a number of specific morphological changes to this organelle on their depletion. We propose a role for this family of proteins in regulating membrane dynamics in the endomembrane system.

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Keywords {πŸ”}

pubmed, article, google, scholar, cas, cell, proteins, yipf, golgi, biol, central, protein, membrane, family, simpson, rab, dublin, complex, access, transport, science, endoplasmic, university, privacy, cookies, content, research, kranjc, nat, brefeldin, reticulum, pathway, secretory, ireland, college, function, publish, search, biology, functional, cells, tilen, dempsey, cagney, jeremy, role, open, nature, chem, human,

Topics {βœ’οΈ}

intermediate compartment/cis-golgi network month download article/chapter gtp-binding proteins related proteome-wide protein quantification subcellular localisation profile cis-golgi-localising yipfs trans-golgi-localising yipfs copi-independent retrograde transport microtubule-dependent retrograde transport rab9-mediated vesicle transport endoplasmic reticulum-derived vesicles related subjects full article pdf membrane traffic membrane protein enriched yipf protein family regulating membrane dynamics privacy choices/manage cookies gtp-binding mutants family-wide characterization high-throughput method itinerant golgi proteins sec4 products involved lippincott-schwartz article kranjc irish research council cis-golgi compartments check access instant access article histochemistry mammalian endoplasmic reticulum cis-snare complex cellular binding partner endoplasmic reticulum dysfunction transport gtpases ypt1p quantifying cell phenotypes european economic area range mass accuracies copii vesicle biogenesis cultured rat hepatocytes threshold selection method gray-level histograms development core team mhc class ii yoshimura s yif1a recycle ethics declarations conflict intracellular vesicle transport cell biology aims er–golgi intermediate

Schema {πŸ—ΊοΈ}

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         headline:Functional characterisation of the YIPF protein family in mammalian cells
         description:In this study, we carry out a systematic characterisation of the YIPF family of proteins with respect to their subcellular localisation profile, membrane topology and functional effects on the endomembrane system. YIPF proteins primarily localise to the Golgi complex and can be grouped into trans-Golgi-localising YIPFs (YIPF1 and YIPF2) and cis-Golgi-localising YIPFs (YIPF3, YIPF4 and YIPF5), with YIPF6 and YIPF7 showing a broader profile being distributed throughout the Golgi stack. YIPF proteins have a long soluble N-terminal region, which is orientated towards the cytosol, followed by 5 closely stacked transmembrane domains, and a C terminus, orientated towards the lumen of the Golgi. The significance of YIPF proteins for the maintenance of the morphology of the Golgi was tested by RNA interference, revealing a number of specific morphological changes to this organelle on their depletion. We propose a role for this family of proteins in regulating membrane dynamics in the endomembrane system.
         datePublished:2016-12-20T00:00:00Z
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      headline:Functional characterisation of the YIPF protein family in mammalian cells
      description:In this study, we carry out a systematic characterisation of the YIPF family of proteins with respect to their subcellular localisation profile, membrane topology and functional effects on the endomembrane system. YIPF proteins primarily localise to the Golgi complex and can be grouped into trans-Golgi-localising YIPFs (YIPF1 and YIPF2) and cis-Golgi-localising YIPFs (YIPF3, YIPF4 and YIPF5), with YIPF6 and YIPF7 showing a broader profile being distributed throughout the Golgi stack. YIPF proteins have a long soluble N-terminal region, which is orientated towards the cytosol, followed by 5 closely stacked transmembrane domains, and a C terminus, orientated towards the lumen of the Golgi. The significance of YIPF proteins for the maintenance of the morphology of the Golgi was tested by RNA interference, revealing a number of specific morphological changes to this organelle on their depletion. We propose a role for this family of proteins in regulating membrane dynamics in the endomembrane system.
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