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Sequence and structural insights of monoleucine-based sorting motifs contained within the cytoplasmic domains of basolateral proteins.
Harmych, Sarah J; Tydings, Claiborne W; Meiler, Jens; Singh, Bhuminder.
Affiliation
  • Harmych SJ; Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, United States.
  • Tydings CW; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN, United States.
  • Meiler J; Department of Chemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN, United States.
  • Singh B; Department of Chemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN, United States.
Front Cell Dev Biol ; 12: 1379224, 2024.
Article in En | MEDLINE | ID: mdl-38495621
ABSTRACT
Delivery to the correct membrane domain in polarized epithelial cells is a critical regulatory mechanism for transmembrane proteins. The trafficking of these proteins is directed by short amino acid sequences known as sorting motifs. In six basolaterally-localized proteins lacking the canonical tyrosine- and dileucine-based basolateral sorting motifs, a monoleucine-based sorting motif has been identified. This review will discuss these proteins with an identified monoleucine-based sorting motif, their conserved structural features, as well as the future directions of study for this non-canonical basolateral sorting motif.
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Front Cell Dev Biol Year: 2024 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Front Cell Dev Biol Year: 2024 Document type: Article Affiliation country: Country of publication: