scholarly journals The transmembrane domain of TACE regulates protein ectodomain shedding

Cell Research ◽  
2007 ◽  
Vol 17 (12) ◽  
pp. 985-998 ◽  
Author(s):  
Xiaojin Li ◽  
Liliana Pérez ◽  
Zui Pan ◽  
Huizhou Fan
Keyword(s):  
Transmembrane Domain ◽  
Ectodomain Shedding ◽  
Protein Ectodomain Shedding

scholarly journals Proteomic changes in cerebrospinal fluid from primary central nervous system lymphoma patients are associated with protein ectodomain shedding

Oncotarget ◽  
2017 ◽  
Vol 8 (66) ◽  
pp. 110118-110132 ◽  
Author(s):  
Daniel Michael Waldera-Lupa ◽  
Omid Etemad-Parishanzadeh ◽  
Mareike Brocksieper ◽  
Nina Kirchgaessler ◽  
Sabine Seidel ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Cerebrospinal Fluid ◽  
Nervous System ◽  
Central Nervous System Lymphoma ◽  
Ectodomain Shedding ◽  
Protein Ectodomain Shedding

Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding

1999 ◽  
Vol 112 (21) ◽  
pp. 3603-3617 ◽  
Author(s):  
J. Schlondorff ◽  
C.P. Blobel
Keyword(s):  
Tumor Necrosis ◽  
Ectodomain Shedding ◽  
Membrane Glycoproteins ◽  
Tnf Α ◽  
Disintegrin Domain ◽  
Protein Ectodomain Shedding ◽  
Integrin Ligands ◽  
Factor Α ◽  
Necrosis Factor

Metalloprotease-disintegrins (ADAMs) have captured our attention as key players in fertilization and in the processing of the ectodomains of proteins such as tumor necrosis factor (α) (TNF(α)), and because of their roles in Notch-mediated signaling, neurogenesis and muscle fusion. ADAMs are integral membrane glycoproteins that contain a disintegrin domain, which is related to snake-venom integrin ligands, and a metalloprotease domain (which can contain or lack a catalytic site). Here, we review and critically discuss current topics in the ADAMs field, including the central role of fertilin in fertilization, the role of the TNF(α) convertase in protein ectodomain processing, the role of Kuzbanian in Notch signaling, and links between ADAMs and processing of the amyloid-precursor protein.

Protein Ectodomain Shedding

2002 ◽  
Vol 102 (12) ◽  
pp. 4627-4638 ◽  
Author(s):  
Joaquín Arribas ◽  
Aldo Borroto
Keyword(s):  
Ectodomain Shedding ◽  
Protein Ectodomain Shedding

scholarly journals Mice with defects in HB-EGF ectodomain shedding show severe developmental abnormalities

2003 ◽  
Vol 163 (3) ◽  
pp. 469-475 ◽  
Author(s):  
Satoru Yamazaki ◽  
Ryo Iwamoto ◽  
Kazuko Saeki ◽  
Masanori Asakura ◽  
Seiji Takashima ◽  
...  
Keyword(s):  
Heart Valves ◽  
Transmembrane Domain ◽  
Severe Heart Failure ◽  
Gene Replacement ◽  
Soluble Form ◽  
Ectodomain Shedding ◽  
Heparin Binding ◽  
Developmental Abnormalities ◽  
Targeted Gene Replacement

Heparin-binding EGF-like growth factor (HB-EGF) is first synthesized as a membrane-anchored form (proHB-EGF), and its soluble form (sHB-EGF) is released by ectodomain shedding from proHB-EGF. To examine the significance of proHB-EGF processing in vivo, we generated mutant mice by targeted gene replacement, expressing either an uncleavable form (HBuc) or a transmembrane domain–truncated form (HBΔtm) of the molecule. HBuc/uc mice developed severe heart failure and enlarged heart valves, phenotypes similar to those in proHB-EGF null mice. On the other hand, mice carrying HBΔtm exhibited severe hyperplasia in both skin and heart. These results indicate that ectodomain shedding of proHB-EGF is essential for HB-EGF function in vivo, and that this process requires strict control.

Protein Ectodomain Shedding

ChemInform ◽  
2003 ◽  
Vol 34 (7) ◽  
Author(s):  
Joaquin Arribas ◽  
Aldo Borroto
Keyword(s):  
Ectodomain Shedding ◽  
Protein Ectodomain Shedding

scholarly journals Substrate‐selective protein ectodomain shedding by ADAM17 and iRhom2 depends on their juxtamembrane and transmembrane domains

2020 ◽  
Vol 34 (4) ◽  
pp. 4956-4969 ◽  
Author(s):  
Beiyu Tang ◽  
Xue Li ◽  
Thorsten Maretzky ◽  
Jose Manuel Perez‐Aguilar ◽  
David McIlwain ◽  
...  
Keyword(s):  
Transmembrane Domains ◽  
Ectodomain Shedding ◽  
Protein Ectodomain Shedding

scholarly journals A quantitative study of the Golgi retention of glycosyltransferases

2021 ◽  
Author(s):  
Xiuping Sun ◽  
Mahajan Divyanshu ◽  
Bing Chen ◽  
Zhiwei Song ◽  
Lei Lu
Keyword(s):  
Transferrin Receptor ◽  
Tumor Necrosis ◽  
Transmembrane Domain ◽  
Tail Length ◽  
Ectodomain Shedding ◽  
Primary Mechanism ◽  
Golgi Retention ◽  
Factor Α ◽  
Export Signal ◽  
Necrosis Factor

How Golgi glycosyltransferases and glycosidases (hereafter glycosyltransferases) localize to the Golgi is still unclear. Here, we first investigated the post-Golgi trafficking of glycosyltransferases. We found that glycosyltransferases can escape the Golgi to the plasma membrane, where they are subsequently endocytosed to the endolysosome. Post-Golgi glycosyltransferases are probably degraded by the ectodomain shedding. We discovered that most glycosyltransferases are not retrieved from post-Golgi sites, indicating that retention but not retrieval should be the primary mechanism for their Golgi localization. We proposed to use the Golgi residence time to quantitatively and systematically study Golgi retention of glycosyltransferases. Various swapping chimeras between ST6GAL1 and either transferrin receptor or tumor necrosis factor α quantitatively revealed the contributions of three regions of ST6GAL1, namely the N-terminal cytosolic tail, transmembrane domain, and ectodomain, to Golgi retention. We found that each of the three regions is sufficient to produce retention in an additive manner. The N-terminal cytosolic tail length negatively affects the Golgi retention of ST6GAL1, similar to the effect of the transmembrane domain. Therefore, the long N-terminal cytosolic tail and transmembrane domain can be a Golgi export signal for transmembrane secretory cargos.

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