Molecular and Cellular Mechanisms of Ectodomain Shedding

Hayashida, Kazutaka; Bartlett, Allison H.; Chen, Ye; Park, Pyong Woo

doi:10.1002/ar.21196

Cited by 45 publications

(66 citation statements)

References 98 publications

(132 reference statements)

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“…The extracellular domains of a number of transmembrane proteins are released from the cell surface as soluble proteins through a regulated proteolytic mechanism called ectodomain shedding (46,47). Only about 2% of cell surface proteins are released from the surface by ectodomain shedding, indicating that cells selectively shed their protein ectodomains (46).…”

Section: Discussionmentioning

confidence: 99%

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Roles for Trafficking and O-Linked Glycosylation in the Turnover of Model Cell Surface Proteins

Karabasheva

Cole

Donaldson

2014

Journal of Biological Chemistry

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Background: Plasma membrane proteins can be degraded by a number of mechanisms. Results: Turnover rates are determined by endocytosis signals and trafficking to lysosomes, ubiquitination, and ectodomain cleavage. Conclusion: Membrane trafficking to lysosomes and proteolysis at the cell surface determine protein half-life. Significance: Learning how plasma membrane proteins are turned over is critical for understanding protein homeostasis.

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Section: Discussionmentioning

confidence: 99%

“…Only about 2% of cell surface proteins are released from the surface by ectodomain shedding, indicating that cells selectively shed their protein ectodomains (46). Cleavage often occurs in a juxtamembrane stalk region adjacent to the membrane anchor (47)(48)(49) and may require an unstructured or extended stalk of minimal length (50).…”

Section: Discussionmentioning

confidence: 99%

Roles for Trafficking and O-Linked Glycosylation in the Turnover of Model Cell Surface Proteins

Karabasheva

Cole

Donaldson

2014

Journal of Biological Chemistry

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“…1A). By ectodomain shedding, they can also regulate the activity of certain growth factors and cytokines such as HB-EGF and TNF-, and membrane-spanning receptors such as c-Met (89)(90)(91).…”

Section: Expression Of Direct-acting Sasp Components Alonementioning

confidence: 99%

Erratum to: From cell senescence to age-related diseases: differential mechanisms of action of senescence-associated secretory phenotypes

et al. 2016

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The BMB Reports would like to correct in the reference of BMB Rep. 48(10), 549-558 titled "From cell senescence to age-related diseases: differential mechanisms of action of senescence-associated secretory phenotypes". The REFERENCE should be corrected as red highlighting in this pages. This Erratum's doi is https://doi.org/10.5483/ BMBRep.2016.49.11.122. Cellular senescence is a process by which cells enter a state of permanent cell cycle arrest. It is commonly believed to underlie organismal aging and age-associated diseases. However, the mechanism by which cellular senescence contributes to aging and age-associated pathologies remains unclear. Recent studies showed that senescent cells exert detrimental effects on the tissue microenvironment, generating pathological facilitators or aggravators. The most significant environmental effector resulting from senescent cells is the senescence-associated secretory phenotype (SASP), which is constituted by a strikingly increased expression and secretion of diverse pro-inflammatory cytokines. Careful investigation into the components of SASPs and their mechanism of action, may improve our understanding of the pathological backgrounds of age-associated diseases. In this review, we focus on the differential expression of SASP-related genes, in addition to SASP components, during the progress of senescence. We also provide a perspective on the possible action mechanisms of SASP components, and potential contributions of SASP-expressing senescent cells, to age-associated pathologies.

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“…The protein a disintegrin and metalloproteinase domain 10 (ADAM10) is a cell surface sheddase that is able to cleave the extracellular domains of membrane-bound proteins and release the soluble ectodomain in a process known as 'ectodomain shedding' (Hayashida et al, 2010;Reiss and Saftig, 2009;Weber and Saftig, 2012). ADAM10 is crucial for the regulation of various physiological processes such as cell proliferation, differentiation and death (Gibb et al, 2011;Glomski et al, 2011;Guo et al, 2015;Jorissen et al, 2010;Tsai et al, 2014;Weber et al, 2011;Zhang et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

ADAM10-Notch signaling governs the recruitment of ovarian pregranulosa cells and controls folliculogenesis in mice

Feng

Wang

Cai

et al. 2016

Journal of Cell Science

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Ovarian follicles are the basic functional units of female reproduction in the mammalian ovary. We show here that the protein a disintegrin and metalloproteinase domain 10 (ADAM10), a cell surface sheddase, plays an indispensable role in controlling primordial follicle formation by regulating the recruitment of follicle supporting cells in mice. We demonstrate that suppressing ADAM10 in vitro or deletion of Adam10 in vivo disrupts germline cyst breakdown and primordial follicle formation. Using a cell lineage tracing approach, we show that ADAM10 governs the recruitment of ovarian follicle cells by regulating the differentiation and proliferation of LGR5-positive follicle supporting progenitor cells. By detecting the development of FOXL2-positive pregranulosa cells, we found that inhibiting ADAM10 reduced the number of FOXL2-positive cells in perinatal ovaries. Furthermore, inhibiting ADAM10 suppressed the activation of Notch signaling, and blocking Notch signaling also disrupted the recruitment of follicle progenitor cells. Taken together, these results show that ADAM10-Notch signaling in ovarian somatic cells governs the primordial follicle formation by controlling the development of ovarian pregranulosa cells. The proper recruitment of ovarian follicle supporting cells is essential for establishment of the ovarian reserve in mice.

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Molecular and Cellular Mechanisms of Ectodomain Shedding

Cited by 45 publications

References 98 publications

Roles for Trafficking and O-Linked Glycosylation in the Turnover of Model Cell Surface Proteins

Roles for Trafficking and O-Linked Glycosylation in the Turnover of Model Cell Surface Proteins

Erratum to: From cell senescence to age-related diseases: differential mechanisms of action of senescence-associated secretory phenotypes

ADAM10-Notch signaling governs the recruitment of ovarian pregranulosa cells and controls folliculogenesis in mice

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