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We began analyzing https://elifesciences.org/articles/11205, but it redirected us to https://elifesciences.org/articles/11205. The analysis below is for the second page.

Title[redir]:
Translocation of interleukin-1β into a vesicle intermediate in autophagy-mediated secretion | eLife
Description:
Cells release a large number of proteins to the extracellular space. The majority of these ‘secreted’ proteins first pass through two structures inside cells called the endoplasmic reticulum and Golgi. However, a growing number of proteins have been identified that are released by an unconventional mechanism that bypasses the endoplasmic reticulum and Golgi. Autophagy is a process that destroys damaged proteins and other unwanted material in cells. It gets triggered when cells are starved of nutrients, leading them to digest their own materials and recycle the resources into new molecules. During autophagy, a cup-like structure with a double layer of membrane forms around the material that is to be digested. This structure then elongates and eventually engulfs the material to form a bubble-like compartment called the autophagosome. Recent evidence has suggested that autophagosomes are involved in the unconventional secretion of a protein called interleukin-1β; this protein is crucial for the body’s immune response against infection. However, it was not clear how these proteins entered the autophagosomes. Zhang et al. have now explored the link between interleukin-1β and autophagy in more detail. The experiments showed that when autophagy was triggered by starvation, the secretion of interleukin-1β was enhanced. Conversely, when autophagy was inhibited, interleukin-1β accumulated inside the cells and could not be secreted. Further experiments then revealed unexpectedly that interleukin-1β was not engulfed by the cup-like structure (as is the case for material that is destined to be removed). Instead, interleukin-1β was found to enter into smaller bubble-like packages (called vesicles) that turn into the autophagosome. Zhang et al. also found that a protein called HSP90 binds to interleukin-1β and enables it to cross the membrane (or translocate) into the vesicles, and that this means that interleukin-1β actually resides in the space between the outer and inner membranes of the autophagosome. How many other proteins share this unusual route out of the cell and what membrane channel is used for this translocation event remain open questions for the future.

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Keywords {🔍}

ilβ, figure, secretion, scholar, google, cells, cell, membrane, autophagosome, protein, mature, hsp, autophagy, unconventional, biology, proteins, journal, membranes, translocation, berkeley, phagophore, vesicle, article, asset, httpsdoiorgelife, data, starvation, download, formation, required, pilβ, hekt, supplement, fraction, open, buffer, pcaspase, performed, proteinase, molecular, elife, min, university, milβ, precursor, cargoes, carrier, atg, antibody, imaging,

Topics {✒️}

excess cytosolic m-il-1β-flag shrna-mediated gene silencing residual dhfr-tagged il-1β n-terminal signal peptide flag-tagged m-il-1β flag-tagged mature il-1β virtual z-section thickness thornberry pcr-based site-directed mutagenesis real-time single-cell imaging plasmid encoding p-il-1β p-il-1β mutants 130-131aa nf-κb signaling cascade autophagy-regulated il-1β secretion p-il-1β-dhfr plasmid glycyl-l-phenylalanine-2-naphthylamide natsume tguan j-lmizushima p300-mediated acetylation stabilizes acousto-optic tunable filter starvation-induced il-1β secretion p-caspase-1 secreted il-1β anti-flag m2 agarose reconstitute autophagy-mediated secretion pew biomedical scholar gtpase-activating proteins tbc1d10a dhfr-tagged il-1β m-il-1β appears interleukin-1β accumulated inside il-1β protein levels pro-il-1β lacks protein g-sepharose beads bi-directional protein transport mouse anti-dhfr antibody m-il-1β-flag autophagy-deficient cell line m-il-1β enters 17 kda mature il-1β secrete mature il-1β mature il-1β appears il-1β secretion downstream induce il-1β secretion autophagy-regulated unconventional secretion cytoplasmic il-1β associates expressing pro-il-1β require m-il-1β il-1β including 127lrdeq131 p2x7 receptor-dependent blebbing precursor il-1β appears multi-protein complex called expressing p-il-1β

Questions {❓}

Manjithaya RSubramani S (2011) Autophagy: a broad role in unconventional protein secretion?
Steringer JPMüller H-MNickel W (2015) Unconventional secretion of fibroblast growth factor 2—a novel type of protein translocation across membranes?

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ScholarlyArticle:
      context:https://schema.org
      mainEntityOfPage:
         type:WebPage
         id:https://elifesciences.org/articles/11205
      headline:Translocation of interleukin-1β into a vesicle intermediate in autophagy-mediated secretion
      datePublished:2015-11-02
      author:
            type:Person
            name:Min Zhang
            type:Person
            name:Samuel J Kenny
            type:Person
            name:Liang Ge
            type:Person
            name:Ke Xu
            type:Person
            name:Randy Schekman
      publisher:
         type:Organization
         name:eLife Sciences Publications, Ltd
         logo:
            type:ImageObject
            url:https://elifesciences.org/assets/patterns/img/patterns/organisms/[email protected]
      keywords:
         autophagy
         unconventional secretion
         interleukin-1β
         HSP90
         autophagosome
      about:
         Biochemistry and Chemical Biology
         Cell Biology
      description:Reconstitution of interleukin-1β secretion in non-macrophage cells implicates how this pro-inflammatory cytokine enters into the unconventional pathway of secretion through autophagy.
      isPartOf:
         type:Periodical
         name:eLife
         issn:2050-084X
WebPage:
      id:https://elifesciences.org/articles/11205
Person:
      name:Min Zhang
      name:Samuel J Kenny
      name:Liang Ge
      name:Ke Xu
      name:Randy Schekman
Organization:
      name:eLife Sciences Publications, Ltd
      logo:
         type:ImageObject
         url:https://elifesciences.org/assets/patterns/img/patterns/organisms/[email protected]
ImageObject:
      url:https://elifesciences.org/assets/patterns/img/patterns/organisms/[email protected]
Periodical:
      name:eLife
      issn:2050-084X

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