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Proteolytic ectodomain shedding of membrane proteins in mammals-hardware, concepts, and recent developments

Lichtenthaler, Stefan F, Lemberg, Marius K, Fluhrer, Regina·2018·The EMBO Journal
DOI 10.15252/embj.201899456
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Crossref · 10.15252/embj.201899456

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  • The shed ectodomain assumes distinct biological functions in an autocrine or paracrine manner.

    “In addition to abolishing the original functions of transmembrane proteins, the shed ectodomain assumes distinct biological functions in an autocrine or a paracrine manner, such as transforming growth factor alpha and tumor necrosis factor alpha (TNFα) (11).”

    From ADAM17 mediates ectodomain shedding of the soluble VLDL receptor fragment in the retinal epithelium (2021) · cites this paper as [11]

    The section “How does shedding alter membrane protein function?” says that shedding can release biologically active TGFα and TNFα ectodomains, and explicitly describes shed TNFα acting in a paracrine manner. It does not describe autocrine action, and presents termination of a membrane protein’s function and release of an active ectodomain as different ways shedding can act, not necessarily simultaneous effects. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • Furin, the third member of the proprotein convertase family, enhances the shedding of various cell-surface proteins at the general PC-like motif (R/K)Xn(R/K) down arrow.

    “Furin, the third member of the proprotein convertase (PC) family (26), has been shown to enhance the shedding of various cell-surface proteins at the general PC-like motif (R/K)Xn(R/K)↓, where Xn represents 0, 2, 4, or 6 spacer aa (27).”

    From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [27]

  • Dysregulated sheddases contribute to pathological changes in human diseases.

    “Dysregulated sheddases contribute to the pathological changes in human diseases (11).”

    From ADAM17 mediates ectodomain shedding of the soluble VLDL receptor fragment in the retinal epithelium (2021) · cites this paper as [11]

  • Recent proteomic studies have identified a number of substrates for various sheddases, but many of them have not yet been validated under sheddase-deficient conditions or via in vivo studies.

    “Recent proteomic studies have identified a number of substrates for various sheddases, but many of them have not yet been validated under sheddase-deficient conditions or via in vivo studies (11).”

    From ADAM17 mediates ectodomain shedding of the soluble VLDL receptor fragment in the retinal epithelium (2021) · cites this paper as [11]

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Metadata

Authors
Lichtenthaler, S. F., Lemberg, M. K., & Fluhrer, R.
ORCID
Venue
The EMBO Journal
Publisher
Springer Science and Business Media LLC
Published
2018-07-05
Volume
37
Issue
15
ISSN
  • 0261-4189
  • 1460-2075
DOI
10.15252/embj.201899456
Cited by
323
References
17
Language
en
Licence
Funders
Deutsche Forschungsgemeinschaft (FOR2290)

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