Ent3p Is a PtdIns(3,5)P2 effector required for protein sorting to the multivesicular body

Autor: Sylvie Friant, Delphine Nourrisson, François Letourneur, Eve Isabelle Pécheur, Anne Eugster, Fabrice Michel, Yaya Lefkir
Přispěvatelé: Friant, Sylvie, Génétique moléculaire, génomique, microbiologie (GMGM), Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Deleage, Gilbert
Jazyk: angličtina
Rok vydání: 2003
Předmět:
Time Factors
Epsin
Vesicular Transport Proteins
Pyridinium Compounds
medicine.disease_cause
MESH: Multienzyme Complexes
MESH: Neuropeptides
Mixed Function Oxygenases
MESH: Protein Structure
Tertiary

MESH: Quaternary Ammonium Compounds
0302 clinical medicine
Phosphatidylinositol Phosphates
Yeasts
Protein targeting
MESH: Precipitin Tests
MESH: Clathrin
ENTH domain
0303 health sciences
biology
MESH: Kinetics
Vacuolar lumen
Temperature
MESH: Mixed Function Oxygenases
MESH: Phosphatidylinositol Phosphates
Endocytosis
Cell biology
Protein Transport
MESH: Pyridinium Compounds
MESH: Endocytosis
MESH: Luminescent Proteins
MESH: Fungal Proteins
MESH: Temp
MESH: Protein Sorting Signals
MESH: Protein Transport
MESH: Mutation
Endosome
Blotting
Western

Green Fluorescent Proteins
MESH: Sequence Alignment
MESH: Carrier Proteins
Endosomes
[SDV.BC]Life Sciences [q-bio]/Cellular Biology
macromolecular substances
In Vitro Techniques
Protein Sorting Signals
MESH: Alkyl and Aryl Transferases
MESH: Actins
Clathrin
General Biochemistry
Genetics and Molecular Biology

Actin cytoskeleton organization
Fungal Proteins
03 medical and health sciences
MESH: Green Fluorescent Proteins
Multienzyme Complexes
medicine
[SDV.BBM] Life Sciences [q-bio]/Biochemistry
Molecular Biology

MESH: Blotting
Western

[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology

Multivesicular Body
Molecular Biology
[SDV.BC] Life Sciences [q-bio]/Cellular Biology
030304 developmental biology
Alkyl and Aryl Transferases
Neuropeptides
Cell Biology
MESH: Adaptor Proteins
Vesicular Transport

Precipitin Tests
Actins
Protein Structure
Tertiary

Quaternary Ammonium Compounds
Adaptor Proteins
Vesicular Transport

Kinetics
Luminescent Proteins
MESH: Endosomes
Mutation
Vacuoles
biology.protein
Carrier Proteins
Sequence Alignment
030217 neurology & neurosurgery
Developmental Biology
Zdroj: Developmental Cell
Developmental Cell, Elsevier, 2003, 5 (3), pp.499-511
Developmental Cell, Elsevier, 2003, 5, pp.499-511
ISSN: 1534-5807
Popis: International audience; PtdIns(3,5)P(2) is required for cargo-selective sorting to the vacuolar lumen via the multivesicular body (MVB). Here we show that Ent3p, a yeast epsin N-terminal homology (ENTH) domain-containing protein, is a specific PtdIns(3,5)P(2) effector localized to endosomes. The ENTH domain of Ent3p is essential for its PtdIns(3,5)P(2) binding activity and for its membrane interaction in vitro and in vivo. Ent3p is required for protein sorting into the MVB but not for the internalization step of endocytosis. Ent3p is associated with clathrin and is necessary for normal actin cytoskeleton organization. Our results show that Ent3p is required for protein sorting into intralumenal vesicles of the MVB through PtdIns(3,5)P(2) binding via its ENTH domain.PtdIns(3,5)P(2) is required for cargo-selective sorting to the vacuolar lumen via the multivesicular body (MVB). Here we show that Ent3p, a yeast epsin N-terminal homology (ENTH) domain-containing protein, is a specific PtdIns(3,5)P(2) effector localized to endosomes. The ENTH domain of Ent3p is essential for its PtdIns(3,5)P(2) binding activity and for its membrane interaction in vitro and in vivo. Ent3p is required for protein sorting into the MVB but not for the internalization step of endocytosis. Ent3p is associated with clathrin and is necessary for normal actin cytoskeleton organization. Our results show that Ent3p is required for protein sorting into intralumenal vesicles of the MVB through PtdIns(3,5)P(2) binding via its ENTH domain.
Databáze: OpenAIRE