The role of the SEA (sea urchin sperm protein, enterokinase and agrin) module in cleavage of membrane‐tethered mucins

@article{PalmaiPallag2005TheRO,
  title={The role of the SEA (sea urchin sperm protein, enterokinase and agrin) module in cleavage of membrane‐tethered mucins},
  author={Timea Palmai-Pallag and Naila Khodabukus and Leo Kinarsky and Shih-Hsing Leir and Simon A. Sherman and Michael A. Hollingsworth and Ann Harris},
  journal={The FEBS Journal},
  year={2005},
  volume={272}
}
The membrane‐tethered mucins are cell surface‐associated dimeric or multimeric molecules with extracellular, transmembrane and cytoplasmic portions, that arise from cleavage of the primary polypeptide chain. Following the first cleavage, which may be cotranslational, the subunits remain closely associated through undefined noncovalent interactions. These mucins all share a common structural motif, the SEA module that is found in many other membrane‐associated proteins that are released from the… 
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References

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TLDR
It is demonstrated that cleavage depends not only on the presence of the G/SIVV site, but also on more distant C-terminal sequences in the SEA (sea-urchin sperm protein, enterokinase and agrin) module, and re-association of the fragments requires the SEA module, but is independent of N-linked oligosaccharides.
C-terminal domain of rodent intestinal mucin Muc3 is proteolytically cleaved in the endoplasmic reticulum to generate extracellular and membrane components.
TLDR
Early proteolytic cleavage may be a conserved characteristic of many membrane-associated mucins, possibly as a prelude to later release of their large extracellular domains at cell surfaces.
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    Protein science : a publication of the Protein Society
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TLDR
Using a variety of homology search methods and multiple alignments, a new extracellular module was identified in agrin, enterokinase, and a 63‐kDa sea urchin sperm protein, which contain all O‐glycosidiclinked carbohydrates such as heparan sulfate that contribute considerably to their molecular masses.
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TLDR
The MUC1 proteolytic cleavage site shows homology with sequences in other cell-surface-associated proteins and may represent a common mechanism for processing of these molecules.
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TLDR
It is hypothesize that all membrane resident proteins containing such a “SEA” module will undergo cleavage, thereby generating a receptor–ligand alliance and could well lead to the rational design and identification of molecules that, by binding to one of the cleaved partners, will act either as agonists or antagonists, alter signal transduction and, hence, cellular behavior.
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TLDR
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TLDR
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TLDR
Nuclear localization of fragments of MUC1 CT in association with β-catenin is demonstrated and the possibility that overexpression of the M UC1 CT stabilizes β-Catenin and enhances levels of nuclear β- catenin during disruption of cadherin-mediated cell-cell adhesion is raised.
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