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Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Prosaposin sorting is mediated by oligomerization.

Libin Yuan1, Carlos R Morales

  • 1Department of Anatomy and Cell Biology, McGill University, 3640 University Street, Montreal, Quebec, Canada H3A 2B2.

Experimental Cell Research
|August 13, 2011
PubMed
Summary
This summary is machine-generated.

Prosaposin protein oligomerization is essential for its secretion from eukaryotic cells. Monomeric prosaposin remains intracellular, while oligomers are secreted, revealing a novel secretory pathway mechanism.

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • Eukaryotic cells utilize complex protein sorting mechanisms.
  • Prosaposin, a precursor to sphingolipid activator proteins, traffics to lysosomes via the trans-Golgi network (TGN).
  • Prosaposin is also secreted extracellularly, but its secretion mechanism is unknown.

Purpose of the Study:

  • To elucidate the mechanism of prosaposin secretion.
  • To investigate the role of prosaposin oligomerization in its cellular trafficking.

Main Methods:

  • Analysis of prosaposin glycosylation states and oligomerization.
  • Investigating the effects of N-terminus and C-terminus deletions on prosaposin trafficking.
  • Studying the interaction of prosaposin with sortilin.

Main Results:

  • Prosaposin forms covalent oligomers, which are secreted extracellularly.
  • Monomeric prosaposin binds to sortilin and remains intracellular.
  • Deletion of the C-terminus does not prevent oligomerization and secretion.
  • Elimination of the N-terminus or saposin domains inhibits oligomerization and leads to intracellular retention.

Conclusions:

  • Prosaposin oligomerization is critical for its entry into the secretory pathway.
  • This study reveals a novel mechanism for protein secretion involving oligomerization.