Deprecated: Optional parameter $limit declared before required parameter $showlink is implicitly treated as a required parameter in /var/www/m_lab.dev.vanderbilt.edu/wp-content/plugins/wp-pubmed-reflist/class.wpPubMedRefList.php on line 27

Deprecated: Optional parameter $subset declared before required parameter $showlink is implicitly treated as a required parameter in /var/www/m_lab.dev.vanderbilt.edu/wp-content/plugins/wp-pubmed-reflist/class.wpPubMedRefList.php on line 27

Notice: Function _load_textdomain_just_in_time was called incorrectly. Translation loading for the sgg domain was triggered too early. This is usually an indicator for some code in the plugin or theme running too early. Translations should be loaded at the init action or later. Please see Debugging in WordPress for more information. (This message was added in version 6.7.0.) in /var/www/m_lab.dev.vanderbilt.edu/wp-includes/functions.php on line 6114
Roles of ubiquitination at the synapse. | Broadie Laboratory | Vanderbilt University Skip to main content

Broadie Laboratory

Roles of ubiquitination at the synapse.

AUTHORS

Haas KFKevin F , Broadie K Kendal . Biochimica et biophysica acta. 2008 8 ; 1779(8). 495-506

ABSTRACT

The ubiquitin proteasome system (UPS) was first described as a mechanism for protein degradation more than three decades ago, but the critical roles of the UPS in regulating neuronal synapses have only recently begun to be revealed. Targeted ubiquitination of synaptic proteins affects multiple facets of the synapse throughout its life cycle; from synaptogenesis and synapse elimination to activity-dependent synaptic plasticity and remodeling. The recent identification of specific UPS molecular pathways that act locally at the synapse illustrates the exquisite specificity of ubiquitination in regulating synaptic protein trafficking and degradation events. Synaptic activity has also been shown to determine the subcellular distribution and composition of the proteasome, providing additional mechanisms for locally regulating synaptic protein degradation. Together these advances reveal that tight control of protein turnover plays a conserved, central role in establishing and modulating synapses in neural circuits.

The ubiquitin proteasome system (UPS) was first described as a mechanism for protein degradation more than three decades ago, but the critical roles of the UPS in regulating neuronal synapses have only recently begun to be revealed. Targeted ubiquitination of synaptic proteins affects multiple facets of the synapse throughout its life cycle; from synaptogenesis and synapse elimination to activity-dependent synaptic plasticity and remodeling. The recent identification of specific UPS molecular pathways that act locally at the synapse illustrates the exquisite specificity of ubiquitination in regulating synaptic protein trafficking and degradation events. Synaptic activity has also been shown to determine the subcellular distribution and composition of the proteasome, providing additional mechanisms for locally regulating synaptic protein degradation. Together these advances reveal that tight control of protein turnover plays a conserved, central role in establishing and modulating synapses in neural circuits.

Tags:

Leave a Response


Warning: Undefined variable $user_ID in /var/www/m_lab.dev.vanderbilt.edu/wp-content/themes/ANCHORDOWN-Vanderbilt/comments.php on line 62