Tomosyn interacts with the SUMO E3 ligase PIASγ.
Protein modification by Small Ubiquitin-like MOdifier (SUMO) entities is involved in a number of neuronal functions, including synaptogenesis and synaptic plasticity. Tomosyn-1 (syntaxin-binding protein 5; STXPB5) binds to t-SNARE (Soluble NSF Attachment Protein Receptor) proteins to regulate neurot...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3948876?pdf=render |
| _version_ | 1819082919178665984 |
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| author | Cornelia J Geerts Linda Jacobsen Rhea van de Bospoort Matthijs Verhage Alexander J A Groffen |
| author_facet | Cornelia J Geerts Linda Jacobsen Rhea van de Bospoort Matthijs Verhage Alexander J A Groffen |
| author_sort | Cornelia J Geerts |
| collection | DOAJ |
| description | Protein modification by Small Ubiquitin-like MOdifier (SUMO) entities is involved in a number of neuronal functions, including synaptogenesis and synaptic plasticity. Tomosyn-1 (syntaxin-binding protein 5; STXPB5) binds to t-SNARE (Soluble NSF Attachment Protein Receptor) proteins to regulate neurotransmission and is one of the few neuronal SUMO substrate proteins identified. Here we used yeast two-hybrid screening to show that tomosyn-1 interacts with the SUMO E3 ligase PIASγ (Protein Inhibitor of Activated STAT; PIAS4 or ZMIZ6). This novel interaction involved the C-terminus of tomosyn-1 and the N-terminus of PIASγ. It was confirmed by two-way immunoprecipitation experiments using the full-length proteins expressed in HEK293T cells. Tomosyn-1 was preferentially modified by the SUMO-2/3 isoform. PIASγ-dependent modification of tomosyn-1 with SUMO-2/3 presents a novel mechanism to adapt secretory strength to the dynamic synaptic environment. |
| first_indexed | 2024-12-21T20:24:19Z |
| format | Article |
| id | doaj.art-a8d4558d20fe499abc8e5d19b602154d |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T20:24:19Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-a8d4558d20fe499abc8e5d19b602154d2022-12-21T18:51:25ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0193e9169710.1371/journal.pone.0091697Tomosyn interacts with the SUMO E3 ligase PIASγ.Cornelia J GeertsLinda JacobsenRhea van de BospoortMatthijs VerhageAlexander J A GroffenProtein modification by Small Ubiquitin-like MOdifier (SUMO) entities is involved in a number of neuronal functions, including synaptogenesis and synaptic plasticity. Tomosyn-1 (syntaxin-binding protein 5; STXPB5) binds to t-SNARE (Soluble NSF Attachment Protein Receptor) proteins to regulate neurotransmission and is one of the few neuronal SUMO substrate proteins identified. Here we used yeast two-hybrid screening to show that tomosyn-1 interacts with the SUMO E3 ligase PIASγ (Protein Inhibitor of Activated STAT; PIAS4 or ZMIZ6). This novel interaction involved the C-terminus of tomosyn-1 and the N-terminus of PIASγ. It was confirmed by two-way immunoprecipitation experiments using the full-length proteins expressed in HEK293T cells. Tomosyn-1 was preferentially modified by the SUMO-2/3 isoform. PIASγ-dependent modification of tomosyn-1 with SUMO-2/3 presents a novel mechanism to adapt secretory strength to the dynamic synaptic environment.http://europepmc.org/articles/PMC3948876?pdf=render |
| spellingShingle | Cornelia J Geerts Linda Jacobsen Rhea van de Bospoort Matthijs Verhage Alexander J A Groffen Tomosyn interacts with the SUMO E3 ligase PIASγ. PLoS ONE |
| title | Tomosyn interacts with the SUMO E3 ligase PIASγ. |
| title_full | Tomosyn interacts with the SUMO E3 ligase PIASγ. |
| title_fullStr | Tomosyn interacts with the SUMO E3 ligase PIASγ. |
| title_full_unstemmed | Tomosyn interacts with the SUMO E3 ligase PIASγ. |
| title_short | Tomosyn interacts with the SUMO E3 ligase PIASγ. |
| title_sort | tomosyn interacts with the sumo e3 ligase piasγ |
| url | http://europepmc.org/articles/PMC3948876?pdf=render |
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