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Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail.

Standard

Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. / Behnke, Jörg; Schneppenheim, Janna; Koch Nolte, Friedrich; Haag, Friedrich; Saftig, Paul; Schröder, Bernd.

in: FEBS LETT, Jahrgang 585, Nr. 19, 19, 2011, S. 2951-2957.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Behnke, J, Schneppenheim, J, Koch Nolte, F, Haag, F, Saftig, P & Schröder, B 2011, 'Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail.', FEBS LETT, Jg. 585, Nr. 19, 19, S. 2951-2957. <http://www.ncbi.nlm.nih.gov/pubmed/21896273?dopt=Citation>

APA

Behnke, J., Schneppenheim, J., Koch Nolte, F., Haag, F., Saftig, P., & Schröder, B. (2011). Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. FEBS LETT, 585(19), 2951-2957. [19]. http://www.ncbi.nlm.nih.gov/pubmed/21896273?dopt=Citation

Vancouver

Behnke J, Schneppenheim J, Koch Nolte F, Haag F, Saftig P, Schröder B. Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. FEBS LETT. 2011;585(19):2951-2957. 19.

Bibtex

@article{75e86815577644318b714aa9d8e1f7b2,
title = "Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail.",
abstract = "Signal-peptide-peptidase-like 2A (SPPL2a), an aspartyl intramembrane protease, has been implicated in the proteolysis of TNF-alpha, Fas Ligand and Bri2. Here, we show that endogenous SPPL2a - in agreement with overexpression studies - is localised in membranes of lysosomes/late endosomes. Furthermore, we have analysed the molecular determinants for lysosomal sorting of SPPL2a by creating chimaeric constructs between SPPL2a and its plasma membrane localised homologue SPPL2b. Lysosomal transport of SPPL2a critically depends on its cytosolic carboxyterminal tail. A canonical tyrosine-based sorting motif of the YXX{\o} type at position 498 is sufficient to direct SPPL2a to lysosomal/late endosomal compartments. This motif accounts for the differential localisation of the homologous proteases SPPL2a and SPPL2b and thereby influences the access to substrates and biological function of SPPL2a.",
keywords = "Animals, Humans, Mice, Molecular Sequence Data, Sequence Alignment, Hela Cells, *Amino Acid Motifs, Aspartic Acid Endopeptidases/*chemistry/genetics/*metabolism, Endosomes/*metabolism, Fibroblasts/cytology/physiology, Lysosomes/*metabolism, Membrane Proteins/genetics/*metabolism, Tyrosine/*metabolism, Animals, Humans, Mice, Molecular Sequence Data, Sequence Alignment, Hela Cells, *Amino Acid Motifs, Aspartic Acid Endopeptidases/*chemistry/genetics/*metabolism, Endosomes/*metabolism, Fibroblasts/cytology/physiology, Lysosomes/*metabolism, Membrane Proteins/genetics/*metabolism, Tyrosine/*metabolism",
author = "J{\"o}rg Behnke and Janna Schneppenheim and {Koch Nolte}, Friedrich and Friedrich Haag and Paul Saftig and Bernd Schr{\"o}der",
year = "2011",
language = "English",
volume = "585",
pages = "2951--2957",
journal = "FEBS LETT",
issn = "0014-5793",
publisher = "Elsevier",
number = "19",

}

RIS

TY - JOUR

T1 - Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail.

AU - Behnke, Jörg

AU - Schneppenheim, Janna

AU - Koch Nolte, Friedrich

AU - Haag, Friedrich

AU - Saftig, Paul

AU - Schröder, Bernd

PY - 2011

Y1 - 2011

N2 - Signal-peptide-peptidase-like 2A (SPPL2a), an aspartyl intramembrane protease, has been implicated in the proteolysis of TNF-alpha, Fas Ligand and Bri2. Here, we show that endogenous SPPL2a - in agreement with overexpression studies - is localised in membranes of lysosomes/late endosomes. Furthermore, we have analysed the molecular determinants for lysosomal sorting of SPPL2a by creating chimaeric constructs between SPPL2a and its plasma membrane localised homologue SPPL2b. Lysosomal transport of SPPL2a critically depends on its cytosolic carboxyterminal tail. A canonical tyrosine-based sorting motif of the YXXø type at position 498 is sufficient to direct SPPL2a to lysosomal/late endosomal compartments. This motif accounts for the differential localisation of the homologous proteases SPPL2a and SPPL2b and thereby influences the access to substrates and biological function of SPPL2a.

AB - Signal-peptide-peptidase-like 2A (SPPL2a), an aspartyl intramembrane protease, has been implicated in the proteolysis of TNF-alpha, Fas Ligand and Bri2. Here, we show that endogenous SPPL2a - in agreement with overexpression studies - is localised in membranes of lysosomes/late endosomes. Furthermore, we have analysed the molecular determinants for lysosomal sorting of SPPL2a by creating chimaeric constructs between SPPL2a and its plasma membrane localised homologue SPPL2b. Lysosomal transport of SPPL2a critically depends on its cytosolic carboxyterminal tail. A canonical tyrosine-based sorting motif of the YXXø type at position 498 is sufficient to direct SPPL2a to lysosomal/late endosomal compartments. This motif accounts for the differential localisation of the homologous proteases SPPL2a and SPPL2b and thereby influences the access to substrates and biological function of SPPL2a.

KW - Animals

KW - Humans

KW - Mice

KW - Molecular Sequence Data

KW - Sequence Alignment

KW - Hela Cells

KW - Amino Acid Motifs

KW - Aspartic Acid Endopeptidases/chemistry/genetics/metabolism

KW - Endosomes/metabolism

KW - Fibroblasts/cytology/physiology

KW - Lysosomes/metabolism

KW - Membrane Proteins/genetics/metabolism

KW - Tyrosine/metabolism

KW - Animals

KW - Humans

KW - Mice

KW - Molecular Sequence Data

KW - Sequence Alignment

KW - Hela Cells

KW - Amino Acid Motifs

KW - Aspartic Acid Endopeptidases/chemistry/genetics/metabolism

KW - Endosomes/metabolism

KW - Fibroblasts/cytology/physiology

KW - Lysosomes/metabolism

KW - Membrane Proteins/genetics/metabolism

KW - Tyrosine/metabolism

M3 - SCORING: Journal article

VL - 585

SP - 2951

EP - 2957

JO - FEBS LETT

JF - FEBS LETT

SN - 0014-5793

IS - 19

M1 - 19

ER -