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Sorting of lysosomal proteins.

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Sorting of lysosomal proteins. / Braulke, Thomas; Bonifacino, Juan S.

In: BBA-MOL CELL RES, Vol. 1793, No. 4, 4, 2009, p. 605-614.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Braulke, T & Bonifacino, JS 2009, 'Sorting of lysosomal proteins.', BBA-MOL CELL RES, vol. 1793, no. 4, 4, pp. 605-614. <http://www.ncbi.nlm.nih.gov/pubmed/19046998?dopt=Citation>

APA

Braulke, T., & Bonifacino, J. S. (2009). Sorting of lysosomal proteins. BBA-MOL CELL RES, 1793(4), 605-614. [4]. http://www.ncbi.nlm.nih.gov/pubmed/19046998?dopt=Citation

Vancouver

Braulke T, Bonifacino JS. Sorting of lysosomal proteins. BBA-MOL CELL RES. 2009;1793(4):605-614. 4.

Bibtex

@article{bf1c1202ba7c4141a458b00243624521,
title = "Sorting of lysosomal proteins.",
abstract = "Lysosomes are composed of soluble and transmembrane proteins that are targeted to lysosomes in a signal-dependent manner. The majority of soluble acid hydrolases are modified with mannose 6-phosphate (M6P) residues, allowing their recognition by M6P receptors in the Golgi complex and ensuing transport to the endosomal/lysosomal system. Other soluble enzymes and non-enzymatic proteins are transported to lysosomes in an M6P-independent manner mediated by alternative receptors such as the lysosomal integral membrane protein LIMP-2 or sortilin. Sorting of cargo receptors and lysosomal transmembrane proteins requires sorting signals present in their cytosolic domains. These signals include dileucine-based motifs, DXXLL or [DE]XXXL[LI], and tyrosine-based motifs, YXX{\O}, which interact with components of clathrin coats such as GGAs or adaptor protein complexes. In addition, phosphorylation and lipid modifications regulate signal recognition and trafficking of lysosomal membrane proteins. The complex interaction of both luminal and cytosolic signals with recognition proteins guarantees the specific and directed transport of proteins to lysosomes.",
keywords = "Animals, Humans, Lysosomes enzymology, Membrane Proteins metabolism, Protein Processing, Post-Translational, Protein Transport, Receptor, IGF Type 2 metabolism, Solubility, Animals, Humans, Lysosomes enzymology, Membrane Proteins metabolism, Protein Processing, Post-Translational, Protein Transport, Receptor, IGF Type 2 metabolism, Solubility",
author = "Thomas Braulke and Bonifacino, {Juan S}",
year = "2009",
language = "Deutsch",
volume = "1793",
pages = "605--614",
journal = "BBA-MOL CELL RES",
issn = "0167-4889",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - Sorting of lysosomal proteins.

AU - Braulke, Thomas

AU - Bonifacino, Juan S

PY - 2009

Y1 - 2009

N2 - Lysosomes are composed of soluble and transmembrane proteins that are targeted to lysosomes in a signal-dependent manner. The majority of soluble acid hydrolases are modified with mannose 6-phosphate (M6P) residues, allowing their recognition by M6P receptors in the Golgi complex and ensuing transport to the endosomal/lysosomal system. Other soluble enzymes and non-enzymatic proteins are transported to lysosomes in an M6P-independent manner mediated by alternative receptors such as the lysosomal integral membrane protein LIMP-2 or sortilin. Sorting of cargo receptors and lysosomal transmembrane proteins requires sorting signals present in their cytosolic domains. These signals include dileucine-based motifs, DXXLL or [DE]XXXL[LI], and tyrosine-based motifs, YXXØ, which interact with components of clathrin coats such as GGAs or adaptor protein complexes. In addition, phosphorylation and lipid modifications regulate signal recognition and trafficking of lysosomal membrane proteins. The complex interaction of both luminal and cytosolic signals with recognition proteins guarantees the specific and directed transport of proteins to lysosomes.

AB - Lysosomes are composed of soluble and transmembrane proteins that are targeted to lysosomes in a signal-dependent manner. The majority of soluble acid hydrolases are modified with mannose 6-phosphate (M6P) residues, allowing their recognition by M6P receptors in the Golgi complex and ensuing transport to the endosomal/lysosomal system. Other soluble enzymes and non-enzymatic proteins are transported to lysosomes in an M6P-independent manner mediated by alternative receptors such as the lysosomal integral membrane protein LIMP-2 or sortilin. Sorting of cargo receptors and lysosomal transmembrane proteins requires sorting signals present in their cytosolic domains. These signals include dileucine-based motifs, DXXLL or [DE]XXXL[LI], and tyrosine-based motifs, YXXØ, which interact with components of clathrin coats such as GGAs or adaptor protein complexes. In addition, phosphorylation and lipid modifications regulate signal recognition and trafficking of lysosomal membrane proteins. The complex interaction of both luminal and cytosolic signals with recognition proteins guarantees the specific and directed transport of proteins to lysosomes.

KW - Animals

KW - Humans

KW - Lysosomes enzymology

KW - Membrane Proteins metabolism

KW - Protein Processing, Post-Translational

KW - Protein Transport

KW - Receptor, IGF Type 2 metabolism

KW - Solubility

KW - Animals

KW - Humans

KW - Lysosomes enzymology

KW - Membrane Proteins metabolism

KW - Protein Processing, Post-Translational

KW - Protein Transport

KW - Receptor, IGF Type 2 metabolism

KW - Solubility

M3 - SCORING: Zeitschriftenaufsatz

VL - 1793

SP - 605

EP - 614

JO - BBA-MOL CELL RES

JF - BBA-MOL CELL RES

SN - 0167-4889

IS - 4

M1 - 4

ER -