Eintrag weiter verarbeiten
The yeast kinase Yck2 has a tripartite palmitoylation signal
Gespeichert in:
| Zeitschriftentitel: | Molecular Biology of the Cell |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Molecular Biology of the Cell, 22, 2011, 15, S. 2702-2715 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Cell Biology (ASCB)
|
| Schlagwörter: |
| author_facet |
Roth, Amy F. Papanayotou, Irene Davis, Nicholas G. Roth, Amy F. Papanayotou, Irene Davis, Nicholas G. |
|---|---|
| author |
Roth, Amy F. Papanayotou, Irene Davis, Nicholas G. |
| spellingShingle |
Roth, Amy F. Papanayotou, Irene Davis, Nicholas G. Molecular Biology of the Cell The yeast kinase Yck2 has a tripartite palmitoylation signal Cell Biology Molecular Biology |
| author_sort |
roth, amy f. |
| spelling |
Roth, Amy F. Papanayotou, Irene Davis, Nicholas G. 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e11-02-0115 <jats:p>The yeast kinase Yck2 tethers to the cytoplasmic surface of the plasma membrane through dual palmitoylation of its C-terminal Cys-Cys dipeptide, mediated by the Golgi-localized palmitoyl-transferase Akr1. Here, the Yck2 palmitoylation signal is found to consist of three parts: 1) a 10-residue-long, conserved C-terminal peptide (CCTP) that includes the C-terminal Cys-Cys dipeptide; 2) the kinase catalytic domain (KD); and mapping between these two elements; and 3) a 176-residue-long, poorly conserved, glutamine-rich sequence. The CCTP, which contains the C-terminal cysteines as well as an important Phe-Phe dipeptide, likely serves as an Akr1 recognition element, because CCTP mutations disrupt palmitoylation within a purified in vitro palmitoylation system. The KD contribution appears to be complex with roles for both KD activity (e.g., Yck2-mediated phosphorylation) and structure (e.g., Akr1 recognition elements). KD and CCTP mutations are strongly synergistic, suggesting that, like the CCTP, the KD may also participate at the Yck2-Akr1 recognition step. The long, glutamine-rich domain, which is located between the KD and CCTP, is predicted to be intrinsically disordered and may function as a flexible, interdomain linker, allowing a coupled interaction of the KD and CCTP with Akr1. Multipart palmitoylation signals may prove to be a general feature of this large class of palmitoylation substrates. These soluble proteins have no clear means of accessing membranes and thus may require active capture out of the cytoplasm for palmitoylation by their membrane-localized transferases.</jats:p> The yeast kinase Yck2 has a tripartite palmitoylation signal Molecular Biology of the Cell |
| doi_str_mv |
10.1091/mbc.e11-02-0115 |
| facet_avail |
Online Free |
| finc_class_facet |
Biologie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA5MS9tYmMuZTExLTAyLTAxMTU |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA5MS9tYmMuZTExLTAyLTAxMTU |
| institution |
DE-D275 DE-Bn3 DE-Brt1 DE-D161 DE-Zwi2 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 |
| imprint |
American Society for Cell Biology (ASCB), 2011 |
| imprint_str_mv |
American Society for Cell Biology (ASCB), 2011 |
| issn |
1059-1524 1939-4586 |
| issn_str_mv |
1059-1524 1939-4586 |
| language |
English |
| mega_collection |
American Society for Cell Biology (ASCB) (CrossRef) |
| match_str |
roth2011theyeastkinaseyck2hasatripartitepalmitoylationsignal |
| publishDateSort |
2011 |
| publisher |
American Society for Cell Biology (ASCB) |
| recordtype |
ai |
| record_format |
ai |
| series |
Molecular Biology of the Cell |
| source_id |
49 |
| title |
The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_unstemmed |
The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_full |
The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_fullStr |
The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_full_unstemmed |
The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_short |
The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_sort |
the yeast kinase yck2 has a tripartite palmitoylation signal |
| topic |
Cell Biology Molecular Biology |
| url |
http://dx.doi.org/10.1091/mbc.e11-02-0115 |
| publishDate |
2011 |
| physical |
2702-2715 |
| description |
<jats:p>The yeast kinase Yck2 tethers to the cytoplasmic surface of the plasma membrane through dual palmitoylation of its C-terminal Cys-Cys dipeptide, mediated by the Golgi-localized palmitoyl-transferase Akr1. Here, the Yck2 palmitoylation signal is found to consist of three parts: 1) a 10-residue-long, conserved C-terminal peptide (CCTP) that includes the C-terminal Cys-Cys dipeptide; 2) the kinase catalytic domain (KD); and mapping between these two elements; and 3) a 176-residue-long, poorly conserved, glutamine-rich sequence. The CCTP, which contains the C-terminal cysteines as well as an important Phe-Phe dipeptide, likely serves as an Akr1 recognition element, because CCTP mutations disrupt palmitoylation within a purified in vitro palmitoylation system. The KD contribution appears to be complex with roles for both KD activity (e.g., Yck2-mediated phosphorylation) and structure (e.g., Akr1 recognition elements). KD and CCTP mutations are strongly synergistic, suggesting that, like the CCTP, the KD may also participate at the Yck2-Akr1 recognition step. The long, glutamine-rich domain, which is located between the KD and CCTP, is predicted to be intrinsically disordered and may function as a flexible, interdomain linker, allowing a coupled interaction of the KD and CCTP with Akr1. Multipart palmitoylation signals may prove to be a general feature of this large class of palmitoylation substrates. These soluble proteins have no clear means of accessing membranes and thus may require active capture out of the cytoplasm for palmitoylation by their membrane-localized transferases.</jats:p> |
| container_issue |
15 |
| container_start_page |
2702 |
| container_title |
Molecular Biology of the Cell |
| container_volume |
22 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792339332043898890 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T15:46:22.62Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=The+yeast+kinase+Yck2+has+a+tripartite+palmitoylation+signal&rft.date=2011-08-01&genre=article&issn=1939-4586&volume=22&issue=15&spage=2702&epage=2715&pages=2702-2715&jtitle=Molecular+Biology+of+the+Cell&atitle=The+yeast+kinase+Yck2+has+a+tripartite+palmitoylation+signal&aulast=Davis&aufirst=Nicholas+G.&rft_id=info%3Adoi%2F10.1091%2Fmbc.e11-02-0115&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792339332043898890 |
| author | Roth, Amy F., Papanayotou, Irene, Davis, Nicholas G. |
| author_facet | Roth, Amy F., Papanayotou, Irene, Davis, Nicholas G., Roth, Amy F., Papanayotou, Irene, Davis, Nicholas G. |
| author_sort | roth, amy f. |
| container_issue | 15 |
| container_start_page | 2702 |
| container_title | Molecular Biology of the Cell |
| container_volume | 22 |
| description | <jats:p>The yeast kinase Yck2 tethers to the cytoplasmic surface of the plasma membrane through dual palmitoylation of its C-terminal Cys-Cys dipeptide, mediated by the Golgi-localized palmitoyl-transferase Akr1. Here, the Yck2 palmitoylation signal is found to consist of three parts: 1) a 10-residue-long, conserved C-terminal peptide (CCTP) that includes the C-terminal Cys-Cys dipeptide; 2) the kinase catalytic domain (KD); and mapping between these two elements; and 3) a 176-residue-long, poorly conserved, glutamine-rich sequence. The CCTP, which contains the C-terminal cysteines as well as an important Phe-Phe dipeptide, likely serves as an Akr1 recognition element, because CCTP mutations disrupt palmitoylation within a purified in vitro palmitoylation system. The KD contribution appears to be complex with roles for both KD activity (e.g., Yck2-mediated phosphorylation) and structure (e.g., Akr1 recognition elements). KD and CCTP mutations are strongly synergistic, suggesting that, like the CCTP, the KD may also participate at the Yck2-Akr1 recognition step. The long, glutamine-rich domain, which is located between the KD and CCTP, is predicted to be intrinsically disordered and may function as a flexible, interdomain linker, allowing a coupled interaction of the KD and CCTP with Akr1. Multipart palmitoylation signals may prove to be a general feature of this large class of palmitoylation substrates. These soluble proteins have no clear means of accessing membranes and thus may require active capture out of the cytoplasm for palmitoylation by their membrane-localized transferases.</jats:p> |
| doi_str_mv | 10.1091/mbc.e11-02-0115 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA5MS9tYmMuZTExLTAyLTAxMTU |
| imprint | American Society for Cell Biology (ASCB), 2011 |
| imprint_str_mv | American Society for Cell Biology (ASCB), 2011 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
| issn | 1059-1524, 1939-4586 |
| issn_str_mv | 1059-1524, 1939-4586 |
| language | English |
| last_indexed | 2024-03-01T15:46:22.62Z |
| match_str | roth2011theyeastkinaseyck2hasatripartitepalmitoylationsignal |
| mega_collection | American Society for Cell Biology (ASCB) (CrossRef) |
| physical | 2702-2715 |
| publishDate | 2011 |
| publishDateSort | 2011 |
| publisher | American Society for Cell Biology (ASCB) |
| record_format | ai |
| recordtype | ai |
| series | Molecular Biology of the Cell |
| source_id | 49 |
| spelling | Roth, Amy F. Papanayotou, Irene Davis, Nicholas G. 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e11-02-0115 <jats:p>The yeast kinase Yck2 tethers to the cytoplasmic surface of the plasma membrane through dual palmitoylation of its C-terminal Cys-Cys dipeptide, mediated by the Golgi-localized palmitoyl-transferase Akr1. Here, the Yck2 palmitoylation signal is found to consist of three parts: 1) a 10-residue-long, conserved C-terminal peptide (CCTP) that includes the C-terminal Cys-Cys dipeptide; 2) the kinase catalytic domain (KD); and mapping between these two elements; and 3) a 176-residue-long, poorly conserved, glutamine-rich sequence. The CCTP, which contains the C-terminal cysteines as well as an important Phe-Phe dipeptide, likely serves as an Akr1 recognition element, because CCTP mutations disrupt palmitoylation within a purified in vitro palmitoylation system. The KD contribution appears to be complex with roles for both KD activity (e.g., Yck2-mediated phosphorylation) and structure (e.g., Akr1 recognition elements). KD and CCTP mutations are strongly synergistic, suggesting that, like the CCTP, the KD may also participate at the Yck2-Akr1 recognition step. The long, glutamine-rich domain, which is located between the KD and CCTP, is predicted to be intrinsically disordered and may function as a flexible, interdomain linker, allowing a coupled interaction of the KD and CCTP with Akr1. Multipart palmitoylation signals may prove to be a general feature of this large class of palmitoylation substrates. These soluble proteins have no clear means of accessing membranes and thus may require active capture out of the cytoplasm for palmitoylation by their membrane-localized transferases.</jats:p> The yeast kinase Yck2 has a tripartite palmitoylation signal Molecular Biology of the Cell |
| spellingShingle | Roth, Amy F., Papanayotou, Irene, Davis, Nicholas G., Molecular Biology of the Cell, The yeast kinase Yck2 has a tripartite palmitoylation signal, Cell Biology, Molecular Biology |
| title | The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_full | The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_fullStr | The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_full_unstemmed | The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_short | The yeast kinase Yck2 has a tripartite palmitoylation signal |
| title_sort | the yeast kinase yck2 has a tripartite palmitoylation signal |
| title_unstemmed | The yeast kinase Yck2 has a tripartite palmitoylation signal |
| topic | Cell Biology, Molecular Biology |
| url | http://dx.doi.org/10.1091/mbc.e11-02-0115 |