A multimeric membrane protein reveals 14-3-3 isoform specificity in forward transport in yeast
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A multimeric membrane protein reveals 14-3-3 isoform specificity in forward transport in yeast. / Michelsen, Kai; Mrowiec, Thomas; Duderstadt, Karl E; Frey, Steffen; Minor, Daniel L; Mayer, Matthias P; Schwappach, Blanche.
in: TRAFFIC, Jahrgang 7, Nr. 7, 07.2006, S. 903-16.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - A multimeric membrane protein reveals 14-3-3 isoform specificity in forward transport in yeast
AU - Michelsen, Kai
AU - Mrowiec, Thomas
AU - Duderstadt, Karl E
AU - Frey, Steffen
AU - Minor, Daniel L
AU - Mayer, Matthias P
AU - Schwappach, Blanche
PY - 2006/7
Y1 - 2006/7
N2 - Arginine (Arg)-based endoplasmic reticulum (ER) localization signals are sorting motifs involved in the quality control of multimeric membrane proteins. They are distinct from other ER localization signals like the C-terminal di-lysine [-K(X)KXX] signal. The Pmp2p isoproteolipid, a type I yeast membrane protein, reports faithfully on the activity of sorting signals when fused to a tail containing either an Arg-based motif or a -KKXX signal. This reporter reveals that the Arg-based ER localization signals from mammalian Kir6.2 and GB1 proteins are functional in yeast. Thus, the machinery involved in recognition of Arg-based signals is evolutionarily conserved. Multimeric presentation of the Arg-based signal from Kir6.2 on Pmp2p results in forward transport, which requires 14-3-3 proteins encoded in yeast by BMH1 and BMH2 in two isoforms. Comparison of a strain without any 14-3-3 proteins (Deltabmh2) and the individual Deltabmh1 or Deltabmh2 shows that the role of 14-3-3 in the trafficking of this multimeric Pmp2p reporter is isoform-specific. Efficient forward transport requires the presence of Bmh1p. The specific role of Bmh1p is not due to differences in abundance or affinity between the isoforms. Our results imply that 14-3-3 proteins mediate forward transport by a mechanism distinct from simple masking of the Arg-based signal.
AB - Arginine (Arg)-based endoplasmic reticulum (ER) localization signals are sorting motifs involved in the quality control of multimeric membrane proteins. They are distinct from other ER localization signals like the C-terminal di-lysine [-K(X)KXX] signal. The Pmp2p isoproteolipid, a type I yeast membrane protein, reports faithfully on the activity of sorting signals when fused to a tail containing either an Arg-based motif or a -KKXX signal. This reporter reveals that the Arg-based ER localization signals from mammalian Kir6.2 and GB1 proteins are functional in yeast. Thus, the machinery involved in recognition of Arg-based signals is evolutionarily conserved. Multimeric presentation of the Arg-based signal from Kir6.2 on Pmp2p results in forward transport, which requires 14-3-3 proteins encoded in yeast by BMH1 and BMH2 in two isoforms. Comparison of a strain without any 14-3-3 proteins (Deltabmh2) and the individual Deltabmh1 or Deltabmh2 shows that the role of 14-3-3 in the trafficking of this multimeric Pmp2p reporter is isoform-specific. Efficient forward transport requires the presence of Bmh1p. The specific role of Bmh1p is not due to differences in abundance or affinity between the isoforms. Our results imply that 14-3-3 proteins mediate forward transport by a mechanism distinct from simple masking of the Arg-based signal.
KW - 14-3-3 Proteins/metabolism
KW - Adaptor Proteins, Signal Transducing
KW - Amino Acid Sequence
KW - Arginine/genetics
KW - Endoplasmic Reticulum/metabolism
KW - Gene Deletion
KW - Gene Dosage
KW - Genes, Reporter/genetics
KW - Membrane Proteins/chemistry
KW - Molecular Sequence Data
KW - Nerve Tissue Proteins/chemistry
KW - Phenotype
KW - Potassium Channels, Inwardly Rectifying/metabolism
KW - Protein Binding
KW - Protein Isoforms/metabolism
KW - Protein Subunits/genetics
KW - Protein Transport
KW - Proteolipids/chemistry
KW - Receptors, GABA/genetics
KW - Saccharomyces cerevisiae/chemistry
KW - Saccharomyces cerevisiae Proteins/chemistry
KW - Signal Transduction
U2 - 10.1111/j.1600-0854.2006.00430.x
DO - 10.1111/j.1600-0854.2006.00430.x
M3 - SCORING: Journal article
C2 - 16734667
VL - 7
SP - 903
EP - 916
JO - TRAFFIC
JF - TRAFFIC
SN - 1398-9219
IS - 7
ER -