Sequence and structural insights of monoleucine-based sorting motifs contained within the cytoplasmic domains of basolateral proteins

被引：0
|
作者：
Harmych, Sarah J. [1 ,2 ]
Tydings, Claiborne W. [3 ,4 ]
Meiler, Jens [3 ,4 ,5 ]
Singh, Bhuminder [1 ,6 ]
机构：
[1] Vanderbilt Univ Sch Med, Dept Med, Nashville, TN 37232 USA
[2] Vanderbilt Univ, Dept Cell & Dev Biol, Nashville, TN USA
[3] Vanderbilt Univ, Dept Chem, Nashville, TN USA
[4] Vanderbilt Univ, Ctr Struct Biol, Nashville, TN USA
[5] Univ Leipzig, Inst Drug Discovery, Med Sch, Leipzig, Germany
[6] Vanderbilt Univ Sch Med, Epithelial Biol Ctr, Nashville, TN 37232 USA
来源：
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY | 2024年 / 12卷
关键词：
epithelial polarity; polarized protein trafficking; basolateral sorting motif; clathrin adaptor proteins; monoleucine-based motif; PLASMA-MEMBRANE; TRAFFICKING; RECOGNITION; POLARITY; SIGNALS; BINDING; AP-1; IDENTIFICATION; LOCALIZATION; EXPLANATION;
D O I：
10.3389/fcell.2024.1379224
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
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.
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页数：8
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