Rules for the recognition of dilysine retrieval motifs by coatomer

Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal s...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Ma, Wenfu [verfasserIn] Goldberg, Jonathan [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2013

Schlagwörter:	coatomer COPI dilysine signal vesicular transport

Anmerkung:	© European Molecular Biology Organization 2013

Übergeordnetes Werk:	Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 32(2013), 7 vom: 12. März, Seite 926-937
Übergeordnetes Werk:	volume:32 ; year:2013 ; number:7 ; day:12 ; month:03 ; pages:926-937

Links:	Volltext

DOI / URN:	10.1038/emboj.2013.41

Katalog-ID:	SPR05786988X

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520			\|a Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α‐COP and β′‐COP bound to a series of naturally occurring retrieval motifs—encompassing KKxx, KxKxx and non‐canonical RKxx and viral KxHxx sequences. Binding experiments show that α‐COP and β′‐COP have generally the same specificity for KKxx and KxKxx, but only β′‐COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side‐chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C‐terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non‐lysine residues.
520			\|a Abstract Transmembrane proteins interact with COPI coatomers for their vesicular Golgi‐ER transport. Crystal structures of the coatomers α‐COP and β′‐COP bound to a series of cargo retrieval motifs uncover the molecular basis of distinct recognition mechanisms.
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912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_161
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912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_252
912			\|a GBV_ILN_266
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
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912			\|a GBV_ILN_702
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912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2018
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
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912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
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912			\|a GBV_ILN_2044
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912			\|a GBV_ILN_2108
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2119
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912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
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912			\|a GBV_ILN_2153
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912			\|a GBV_ILN_2336
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912			\|a GBV_ILN_2522
912			\|a GBV_ILN_2548
912			\|a GBV_ILN_4012
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912			\|a GBV_ILN_4035
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publishDate	2013
allfields	10.1038/emboj.2013.41 doi (DE-627)SPR05786988X (SPR)emboj.2013.41-e DE-627 ger DE-627 rakwb eng Ma, Wenfu verfasserin aut Rules for the recognition of dilysine retrieval motifs by coatomer 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2013 Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α‐COP and β′‐COP bound to a series of naturally occurring retrieval motifs—encompassing KKxx, KxKxx and non‐canonical RKxx and viral KxHxx sequences. Binding experiments show that α‐COP and β′‐COP have generally the same specificity for KKxx and KxKxx, but only β′‐COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side‐chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C‐terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non‐lysine residues. Abstract Transmembrane proteins interact with COPI coatomers for their vesicular Golgi‐ER transport. Crystal structures of the coatomers α‐COP and β′‐COP bound to a series of cargo retrieval motifs uncover the molecular basis of distinct recognition mechanisms. coatomer (dpeaa)DE-He213 COPI (dpeaa)DE-He213 dilysine signal (dpeaa)DE-He213 vesicular transport (dpeaa)DE-He213 Goldberg, Jonathan verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 32(2013), 7 vom: 12. März, Seite 926-937 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:32 year:2013 number:7 day:12 month:03 pages:926-937 https://dx.doi.org/10.1038/emboj.2013.41 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 32 2013 7 12 03 926-937
spelling	10.1038/emboj.2013.41 doi (DE-627)SPR05786988X (SPR)emboj.2013.41-e DE-627 ger DE-627 rakwb eng Ma, Wenfu verfasserin aut Rules for the recognition of dilysine retrieval motifs by coatomer 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2013 Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α‐COP and β′‐COP bound to a series of naturally occurring retrieval motifs—encompassing KKxx, KxKxx and non‐canonical RKxx and viral KxHxx sequences. Binding experiments show that α‐COP and β′‐COP have generally the same specificity for KKxx and KxKxx, but only β′‐COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side‐chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C‐terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non‐lysine residues. Abstract Transmembrane proteins interact with COPI coatomers for their vesicular Golgi‐ER transport. Crystal structures of the coatomers α‐COP and β′‐COP bound to a series of cargo retrieval motifs uncover the molecular basis of distinct recognition mechanisms. coatomer (dpeaa)DE-He213 COPI (dpeaa)DE-He213 dilysine signal (dpeaa)DE-He213 vesicular transport (dpeaa)DE-He213 Goldberg, Jonathan verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 32(2013), 7 vom: 12. März, Seite 926-937 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:32 year:2013 number:7 day:12 month:03 pages:926-937 https://dx.doi.org/10.1038/emboj.2013.41 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 32 2013 7 12 03 926-937
allfields_unstemmed	10.1038/emboj.2013.41 doi (DE-627)SPR05786988X (SPR)emboj.2013.41-e DE-627 ger DE-627 rakwb eng Ma, Wenfu verfasserin aut Rules for the recognition of dilysine retrieval motifs by coatomer 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2013 Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α‐COP and β′‐COP bound to a series of naturally occurring retrieval motifs—encompassing KKxx, KxKxx and non‐canonical RKxx and viral KxHxx sequences. Binding experiments show that α‐COP and β′‐COP have generally the same specificity for KKxx and KxKxx, but only β′‐COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side‐chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C‐terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non‐lysine residues. Abstract Transmembrane proteins interact with COPI coatomers for their vesicular Golgi‐ER transport. Crystal structures of the coatomers α‐COP and β′‐COP bound to a series of cargo retrieval motifs uncover the molecular basis of distinct recognition mechanisms. coatomer (dpeaa)DE-He213 COPI (dpeaa)DE-He213 dilysine signal (dpeaa)DE-He213 vesicular transport (dpeaa)DE-He213 Goldberg, Jonathan verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 32(2013), 7 vom: 12. März, Seite 926-937 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:32 year:2013 number:7 day:12 month:03 pages:926-937 https://dx.doi.org/10.1038/emboj.2013.41 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 32 2013 7 12 03 926-937
allfieldsGer	10.1038/emboj.2013.41 doi (DE-627)SPR05786988X (SPR)emboj.2013.41-e DE-627 ger DE-627 rakwb eng Ma, Wenfu verfasserin aut Rules for the recognition of dilysine retrieval motifs by coatomer 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2013 Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α‐COP and β′‐COP bound to a series of naturally occurring retrieval motifs—encompassing KKxx, KxKxx and non‐canonical RKxx and viral KxHxx sequences. Binding experiments show that α‐COP and β′‐COP have generally the same specificity for KKxx and KxKxx, but only β′‐COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side‐chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C‐terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non‐lysine residues. Abstract Transmembrane proteins interact with COPI coatomers for their vesicular Golgi‐ER transport. Crystal structures of the coatomers α‐COP and β′‐COP bound to a series of cargo retrieval motifs uncover the molecular basis of distinct recognition mechanisms. coatomer (dpeaa)DE-He213 COPI (dpeaa)DE-He213 dilysine signal (dpeaa)DE-He213 vesicular transport (dpeaa)DE-He213 Goldberg, Jonathan verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 32(2013), 7 vom: 12. März, Seite 926-937 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:32 year:2013 number:7 day:12 month:03 pages:926-937 https://dx.doi.org/10.1038/emboj.2013.41 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 32 2013 7 12 03 926-937
allfieldsSound	10.1038/emboj.2013.41 doi (DE-627)SPR05786988X (SPR)emboj.2013.41-e DE-627 ger DE-627 rakwb eng Ma, Wenfu verfasserin aut Rules for the recognition of dilysine retrieval motifs by coatomer 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2013 Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α‐COP and β′‐COP bound to a series of naturally occurring retrieval motifs—encompassing KKxx, KxKxx and non‐canonical RKxx and viral KxHxx sequences. Binding experiments show that α‐COP and β′‐COP have generally the same specificity for KKxx and KxKxx, but only β′‐COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side‐chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C‐terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non‐lysine residues. Abstract Transmembrane proteins interact with COPI coatomers for their vesicular Golgi‐ER transport. Crystal structures of the coatomers α‐COP and β′‐COP bound to a series of cargo retrieval motifs uncover the molecular basis of distinct recognition mechanisms. coatomer (dpeaa)DE-He213 COPI (dpeaa)DE-He213 dilysine signal (dpeaa)DE-He213 vesicular transport (dpeaa)DE-He213 Goldberg, Jonathan verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 32(2013), 7 vom: 12. März, Seite 926-937 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:32 year:2013 number:7 day:12 month:03 pages:926-937 https://dx.doi.org/10.1038/emboj.2013.41 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 32 2013 7 12 03 926-937
language	English
source	Enthalten in The EMBO Journal 32(2013), 7 vom: 12. März, Seite 926-937 volume:32 year:2013 number:7 day:12 month:03 pages:926-937
sourceStr	Enthalten in The EMBO Journal 32(2013), 7 vom: 12. März, Seite 926-937 volume:32 year:2013 number:7 day:12 month:03 pages:926-937
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	coatomer COPI dilysine signal vesicular transport
isfreeaccess_bool	false
container_title	The EMBO Journal
authorswithroles_txt_mv	Ma, Wenfu @@aut@@ Goldberg, Jonathan @@aut@@
publishDateDaySort_date	2013-03-12T00:00:00Z
hierarchy_top_id	266022529
id	SPR05786988X
language_de	englisch
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author	Ma, Wenfu
spellingShingle	Ma, Wenfu misc coatomer misc COPI misc dilysine signal misc vesicular transport Rules for the recognition of dilysine retrieval motifs by coatomer
authorStr	Ma, Wenfu
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topic_title	Rules for the recognition of dilysine retrieval motifs by coatomer coatomer (dpeaa)DE-He213 COPI (dpeaa)DE-He213 dilysine signal (dpeaa)DE-He213 vesicular transport (dpeaa)DE-He213
topic	misc coatomer misc COPI misc dilysine signal misc vesicular transport
topic_unstemmed	misc coatomer misc COPI misc dilysine signal misc vesicular transport
topic_browse	misc coatomer misc COPI misc dilysine signal misc vesicular transport
format_facet	Elektronische Aufsätze Aufsätze Elektronische Ressource
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title	Rules for the recognition of dilysine retrieval motifs by coatomer
ctrlnum	(DE-627)SPR05786988X (SPR)emboj.2013.41-e
title_full	Rules for the recognition of dilysine retrieval motifs by coatomer
author_sort	Ma, Wenfu
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author_browse	Ma, Wenfu Goldberg, Jonathan
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doi_str_mv	10.1038/emboj.2013.41
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title_sort	rules for the recognition of dilysine retrieval motifs by coatomer
title_auth	Rules for the recognition of dilysine retrieval motifs by coatomer
abstract	Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α‐COP and β′‐COP bound to a series of naturally occurring retrieval motifs—encompassing KKxx, KxKxx and non‐canonical RKxx and viral KxHxx sequences. Binding experiments show that α‐COP and β′‐COP have generally the same specificity for KKxx and KxKxx, but only β′‐COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side‐chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C‐terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non‐lysine residues. Abstract Transmembrane proteins interact with COPI coatomers for their vesicular Golgi‐ER transport. Crystal structures of the coatomers α‐COP and β′‐COP bound to a series of cargo retrieval motifs uncover the molecular basis of distinct recognition mechanisms. © European Molecular Biology Organization 2013
abstractGer	Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α‐COP and β′‐COP bound to a series of naturally occurring retrieval motifs—encompassing KKxx, KxKxx and non‐canonical RKxx and viral KxHxx sequences. Binding experiments show that α‐COP and β′‐COP have generally the same specificity for KKxx and KxKxx, but only β′‐COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side‐chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C‐terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non‐lysine residues. Abstract Transmembrane proteins interact with COPI coatomers for their vesicular Golgi‐ER transport. Crystal structures of the coatomers α‐COP and β′‐COP bound to a series of cargo retrieval motifs uncover the molecular basis of distinct recognition mechanisms. © European Molecular Biology Organization 2013
abstract_unstemmed	Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α‐COP and β′‐COP bound to a series of naturally occurring retrieval motifs—encompassing KKxx, KxKxx and non‐canonical RKxx and viral KxHxx sequences. Binding experiments show that α‐COP and β′‐COP have generally the same specificity for KKxx and KxKxx, but only β′‐COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side‐chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C‐terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non‐lysine residues. Abstract Transmembrane proteins interact with COPI coatomers for their vesicular Golgi‐ER transport. Crystal structures of the coatomers α‐COP and β′‐COP bound to a series of cargo retrieval motifs uncover the molecular basis of distinct recognition mechanisms. © European Molecular Biology Organization 2013
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title_short	Rules for the recognition of dilysine retrieval motifs by coatomer
url	https://dx.doi.org/10.1038/emboj.2013.41
remote_bool	true
author2	Goldberg, Jonathan
author2Str	Goldberg, Jonathan
ppnlink	266022529
mediatype_str_mv	c
isOA_txt	false
hochschulschrift_bool	false
doi_str	10.1038/emboj.2013.41
up_date	2024-10-18T04:52:28.106Z
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fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR05786988X</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20241018064938.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">241018s2013 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1038/emboj.2013.41</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR05786988X</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)emboj.2013.41-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Ma, Wenfu</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Rules for the recognition of dilysine retrieval motifs by coatomer</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2013</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© European Molecular Biology Organization 2013</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α‐COP and β′‐COP subunits and packaged into COPI‐coated vesicles for Golgi‐to‐ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α‐COP and β′‐COP bound to a series of naturally occurring retrieval motifs—encompassing KKxx, KxKxx and non‐canonical RKxx and viral KxHxx sequences. Binding experiments show that α‐COP and β′‐COP have generally the same specificity for KKxx and KxKxx, but only β′‐COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side‐chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. 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