ArticleMolecular biology of the cell1998
An atypical sorting determinant in the cytoplasmic domain of P-selectin mediates endosomal sorting.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- A synonymous codon change alters the drug sensitivity of ΔF508 cystic fibrosis transmembrane conductance regulator.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
- Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin.Molecular biology of the cell · 2004Article
- Rapid transport of internalized P-selectin to late endosomes and the TGN: roles in regulating cell surface expression and recycling to secretory granules.The Journal of cell biology · 2000Article
- Down-regulation of cell surface receptors is modulated by polar residues within the transmembrane domain.Molecular biology of the cell · 2000Article
- Sorting to synaptic-like microvesicles from early and late endosomes requires overlapping but not identical targeting signals.Molecular biology of the cell · 2000Article
- Secretagogue-triggered transfer of membrane proteins from neuroendocrine secretory granules to synaptic-like microvesicles.Molecular biology of the cell · 1999Article
- A complex web of signal-dependent trafficking underlies the triorganellar distribution of P-selectin in neuroendocrine PC12 cells.The Journal of cell biology · 1999Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We previously identified the 11 amino acid C1 region of the cytoplasmic domain of P-selectin as essential for an endosomal sorting event that confers rapid turnover on P-selectin. The amino acid sequence of this region has no obvious similarity to other known sorting motifs. We have analyzed the sequence requirements for endosomal sorting by measuring the effects of site-specific mutations on the turnover of P-selectin and of the chimeric protein LLP, containing the lumenal and transmembrane domains of the low density lipoprotein receptor and the cytoplasmic domain of P-selectin. Endosomal sorting activity was remarkably tolerant of alanine substitutions within the C1 region. The activity was eliminated by alanine substitution of only one amino acid residue, leucine 768, where substitution with several other large side chains, hydrophobic and polar, maintained the sorting activity. The results indicate that the endosomal sorting determinant is not structurally related to previously reported sorting determinants. Rather, the results suggest that the structure of the sorting determinant is dependent on the tertiary structure of the cytoplasmic domain.
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