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Human Interaction Network Ontology
| Preferred Name | Fibrillin C-terminal processing | |
| Synonyms |
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| Definitions |
Extracellular deposition of fibrillin requires removal of the C-terminus, which can be cleaved in vitro by several furin/PACE family convertases (Raghunath et al. 1999, Ritty et al. 1999) in a process that is inhibited by N-glycosylation and calreticulin (Ashworth et al. 1999). Furin (PACE) is a transmembrane protein, synthesized as a 100 kDa protein, which rapidly undergoes autocatalytic cleavage to a 94 kDa protein in the endoplasmic reticulum (ER). The propeptide remains bound as an auto-inhibitor. Propeptide release occurs in the acidic pH of the trans-golgi-network (TGN)/endosomal compartment, activating furin. Though furin is primarily localized to the TGN a proportion of furin molecules are found on the cell surface (Teuchert et al. 1999). Profibrillin-1 processing does not occur in the TGN, where it is bound by two ER-resident molecular chaperones, BiP and GRP94. Instead activation by furin occurs as profibrillin-1 is secreted, or immediately after secretion (Wallis et al. 2003). Edited: Jupe, S, 2012-11-12 Authored: Jupe, S, 2012-04-30 Reviewed: Muiznieks, Lisa, 2012-11-02 |
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| ID |
http://purl.obolibrary.org/obo/HINO_0021677 |
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| comment |
Extracellular deposition of fibrillin requires removal of the C-terminus, which can be cleaved in vitro by several furin/PACE family convertases (Raghunath et al. 1999, Ritty et al. 1999) in a process that is inhibited by N-glycosylation and calreticulin (Ashworth et al. 1999). Furin (PACE) is a transmembrane protein, synthesized as a 100 kDa protein, which rapidly undergoes autocatalytic cleavage to a 94 kDa protein in the endoplasmic reticulum (ER). The propeptide remains bound as an auto-inhibitor. Propeptide release occurs in the acidic pH of the trans-golgi-network (TGN)/endosomal compartment, activating furin. Though furin is primarily localized to the TGN a proportion of furin molecules are found on the cell surface (Teuchert et al. 1999). Profibrillin-1 processing does not occur in the TGN, where it is bound by two ER-resident molecular chaperones, BiP and GRP94. Instead activation by furin occurs as profibrillin-1 is secreted, or immediately after secretion (Wallis et al. 2003). Edited: Jupe, S, 2012-11-12 Authored: Jupe, S, 2012-04-30 Reviewed: Muiznieks, Lisa, 2012-11-02
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| definition source |
Pubmed10085138 Reactome, http://www.reactome.org Pubmed10198291 Pubmed10547375 Pubmed14523997 Pubmed10593987
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| label |
Fibrillin C-terminal processing
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| prefixIRI |
HINO:0021677
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| prefLabel |
Fibrillin C-terminal processing
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| seeAlso |
EC Number: 3.4.21 Reactome Database ID Release 432129357 ReactomeREACT_150177
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