NDLI: Identification and characterization of a lysosomal transporter for small neutral amino acids

Content Provider	PubMed Central
Author	Corinne, Sagné Agulhon, Cendra Philippe, Ravassard Darmon, Michèle Hamon, Michel Salah, El Mestikawy Gasnier, Bruno Giros, Bruno
Copyright Year	2001
Abstract	In eukaryotic cells, lysosomes represent a major site for macromolecule degradation. Hydrolysis products are eventually exported from this acidic organelle into the cytosol through specific transporters. Impairment of this process at either the hydrolysis or the efflux step is responsible of several lysosomal storage diseases. However, most lysosomal transporters, although biochemically characterized, remain unknown at the molecular level. In this study, we report the molecular and functional characterization of a lysosomal amino acid transporter (LYAAT-1), remotely related to a family of H+-coupled plasma membrane and synaptic vesicle amino acid transporters. LYAAT-1 is expressed in most rat tissues, with highest levels in the brain where it is present in neurons. Upon overexpression in COS-7 cells, the recombinant protein mediates the accumulation of neutral amino acids, such as γ-aminobutyric acid, l-alanine, and l-proline, through an H+/amino acid symport. Confocal microscopy on brain sections revealed that this transporter colocalizes with cathepsin D, an established lysosomal marker. LYAAT-1 thus appears as a lysosomal transporter that actively exports neutral amino acids from lysosomes by chemiosmotic coupling to the H+-ATPase of these organelles. Homology searching in eukaryotic genomes suggests that LYAAT-1 defines a subgroup of lysosomal transporters in the amino acid/auxin permease family.
Related Links	http://dx.doi.org/10.1073/pnas.121183498
Starting Page	7206
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	13
Volume Number	98
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2001-06-19
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Identification and characterization of a lysosomal transporter for small neutral amino acids.

Characterization of the rat neutral and basic amino acid transporter utilizing anti-peptide antibodies.

Identification and characterization of an amino acid transporter expressed differentially in liver

Identification of a Disulfide Bridge Important for Transport Function of SNAT4 Neutral Amino Acid Transporter

Characterization of the promoter region of the gene for the rat neutral and basic amino acid transporter and chromosomal localization of the human gene.

Expression cloning of a Na(+)-independent neutral amino acid transporter from rat kidney.

Seed and vascular expression of a high-affinity transporter for cationic amino acids in Arabidopsis.

Ultrastructural localization of a neutral and basic amino acid transporter in rat kidney and intestine.

Na+-FACILITATED REACTIONS OF NEUTRAL AMINO ACIDS WITH A CATIONIC AMINO ACID TRANSPORT SYSTEM *

Identification and characterization of a lysosomal transporter for small neutral amino acids

Similar Documents

Identification and characterization of a lysosomal transporter for small neutral amino acids.

Characterization of the rat neutral and basic amino acid transporter utilizing anti-peptide antibodies.

Identification and characterization of an amino acid transporter expressed differentially in liver

Identification of a Disulfide Bridge Important for Transport Function of SNAT4 Neutral Amino Acid Transporter

Characterization of the promoter region of the gene for the rat neutral and basic amino acid transporter and chromosomal localization of the human gene.

Expression cloning of a Na(+)-independent neutral amino acid transporter from rat kidney.

Seed and vascular expression of a high-affinity transporter for cationic amino acids in Arabidopsis.

Ultrastructural localization of a neutral and basic amino acid transporter in rat kidney and intestine.

Na+-FACILITATED REACTIONS OF NEUTRAL AMINO ACIDS WITH A CATIONIC AMINO ACID TRANSPORT SYSTEM *

Identification and characterization of a lysosomal transporter for small neutral amino acids