Expression and distribution of phocein and members of the striatin family in neurones of rat peripheral ganglia

Blondeau, Claude; Gaillard, Stéphane; Ternaux, Jean‐Pierre; Monneron, Ariane; Baude, Agnès

doi:10.1007/s00418-003-0503-x

Cited by 13 publications

(12 citation statements)

References 18 publications

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“…Furthermore, in the spinal cord, motoneurons strongly express both proteins ( Figure 5). It is also known that striatin and SG2NA are both expressed in the soma of the same sensory neurons (11). Altogether, these data show that the expression of at least two proteins of the striatin family occurs in the same neuron.…”

Section: Discussionsupporting

confidence: 65%

“…In mammals, this family consists of three scaffolding proteins composed of striatin, SG2NA and zinedin. They are mainly expressed in the cytoplasm of neurons of both the central and the peripheral nervous system (9)(10)(11). Ultrastructural studies show that striatin is strictly localized to the somatodendritic compartment of neurons and highly concentrated within the spines of the striatal GABAergic neurons (12).…”

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Targeting of Proteins of the Striatin Family to Dendritic Spines: Role of the Coiled‐Coil Domain

Gaillard

Bailly

Benoist

et al. 2005

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Striatin, SG2NA and zinedin, the three mammalian members of the striatin family are multimodular WD-repeat, calmodulin and calveolin-binding proteins. These scaffolding proteins, involved in both signaling and trafficking, are highly expressed in neurons. Using ultrastructural immunolabeling, we showed that, in Purkinje cells and hippocampal neurons, SG2NA is confined to the somatodendritic compartment with the highest density in dendritic spines. In cultured hippocampal neurons, SG2NA is also highly concentrated in dendritic spines. By expressing truncated forms of HA-tagged SG2NAb, we demonstrated that the coiled-coil domain plays an essential role in the targeting of SG2NA within spines. Furthermore, co-immunoprecipitation experiments indicate that this coiled-coil domain is also crucial for the homo-and hetero-oligomerization of these proteins. Thus, oligomerization of the striatin family proteins is probably an obligatory step for their routing to the dendritic spines, and hetero-oligomerization explains why all these proteins are often co-expressed in the neurons of the rat brain and spinal cord. In the central nervous system, most excitatory terminals contact dendritic actin-rich protrusions called dendritic spines. The formation and maintenance of spines, including the postsynaptic components, requires precise targeting and coordinated activation of structural and signaling molecules (1-3). The mechanisms by which scaffolding proteins are sorted into pre-or postsynaptic compartments remain largely unclear. Multi-protein complexes, vesicles and organelles found at axon terminals and dendritic spines are transported by motor proteins along microtubules (4,5). Numerous proteins located in the postsynaptic density (PSD) undergo vesicular transport to dendritic spines in association with neurotransmitter receptors (6). Although the routing motifs of several trans-membrane proteins such as ionotropic glutamate receptors have been identified (7,8), much less is known about the targeting of soluble cytoplasmic proteins to dendritic spines, especially for proteins that do not belong to the PSD. To investigate this problem, we analyzed the routing mechanisms of cytoplasmic, non-PSD-associated, dendritic spine proteins: the striatin family.In mammals, this family consists of three scaffolding proteins composed of striatin, SG2NA and zinedin. They are mainly expressed in the cytoplasm of neurons of both the central and the peripheral nervous system (9-11). Ultrastructural studies show that striatin is strictly localized to the somatodendritic compartment of neurons and highly concentrated within the spines of the striatal GABAergic neurons (12). Information concerning the physiological role of the striatin family is beginning to emerge. First, we have shown that striatin expression is crucial for both dendritic growth in cultured rat embryonic motoneurons and for the control of motor function in adult rats (13). Second, striatin and SG2NA have been proposed to be regulatory subunits of protein phosphatase 2A (14). I...

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Section: Discussionsupporting

confidence: 65%

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Targeting of Proteins of the Striatin Family to Dendritic Spines: Role of the Coiled‐Coil Domain

Gaillard

Bailly

Benoist

et al. 2005

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“…The direct interaction of phocein with SG2NA or other striatin family members, like striatin itself and zinedin, has been validated at the molecular level (Baillat et al,2002). The striatin family of proteins is a family of scaffolding proteins comprising striatin, SG2NA, and zinedin, recently described in peripheral and central neurons (Castets et al,1996, 2000; Blondeau et al,2003). Although their precise physiological function(s) are not yet understood, these proteins, like other scaffolding proteins, are likely to be involved in precise targeting and coordinated activation of structural and signaling molecules in postsynaptic structures.…”

Section: Discussionmentioning

confidence: 99%

“…Along this line, phocein has been shown to interact directly with proteins of the striatin family, including the SG2 nuclear autoantigen SG2NA and zinedin (Baillat et al,2001). These proteins are mainly expressed in brain and peripheral neurons (Castets et al,2000; Blondeau et al,2003), and as such are thought to play a dual role in endocytic processes and in neuronal signaling due to their multiple protein–protein interaction domains (Castets et al,1996; Bartoli et al,1998; Moreno et al,2000; Gaillard et al,2001). Striatin‐deficient neurons display atrophic dendrites in vitro and the transient and specific downregulation of striatin in rat striata is accompanied by a decrease in locomotor activity (Bartoli et al,1999).…”

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Immunogold localization of phocein in dendritic spines

Haeberlé

Castets

Bombarde

et al. 2006

J of Comparative Neurology

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Phocein, a widely expressed intracellular protein involved in clathrin- and dynamin-dependent membrane dynamics, has been shown to interact with members of the striatin family of proteins, striatin, SG2NA, and zinedin. Immunogold labeling was performed to assess subcellular localization of phocein in neurons of the rodent cerebellar cortex and hippocampal Ammon's horn. Most of the phocein-bound gold particles were located within dendritic thorns and spines of the cerebellar Purkinje cells and hippocampal pyramidal neurons, as observed previously for striatin in striatal neurons. The postsynaptic profiles containing phocein were engaged in asymmetric synapses with the main types of afferents in the cerebellum and in the hippocampus. In the cerebellum, phocein-bound immunogold particle numbers ranged from 1-20 in approximately 50% of the Purkinje cell spines. In these spines most of the immunogold particles were found in the neuroplasm ( approximately 70%) and on nonsynaptic plasma membrane domains and related structures such as endocytic-like profiles ( approximately 18%). As soon as the first postnatal week, phocein was detected in the Purkinje cell somatic and dendritic thorns making asymmetric synapses with climbing fibers. During the following weeks the protein was located in the dendritic spines, as observed in the adult molecular layer. Finally, double immunogold labeling revealed a distribution of phocein and SG2NA suggesting that the two proteins could interact in the Purkinje cell spines. The early postnatal expression of phocein, a protein involved in membrane dynamics, suggests that it may have functional relevance in dendritic remodeling during development and potentially in spine plasticity during adulthood.

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“…Zinedin (also called striatin 4), a member of the striatin family, is a cytoplasmic protein specifically expressed in the central and peripheral nervous systems (Castets et al 2000;Blondeau et al 2003). At the molecular level, the proteins of the striatin family (zinedin, striatin and SG2NA) share four identical protein-protein interaction domains: from the N to the C-termini, a caveolin-binding domain (Gaillard et al 2001), a coiled-coil structure ), a Ca 2+ -calmodulin-binding domain ) and a large WD-repeat-domain in the C-terminal moiety of these proteins.…”

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Distribution of zinedin in the rat brain

Benoist

Baude

Tasmadjian

et al. 2008

Journal of Neurochemistry

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Members of the striatin family are scaffolding proteins involved in numerous signaling pathways principally in neurons. Zinedin is the only member of this protein family for which the brain distribution has not been determined so far. Here, we have validated a specific antibody against zinedin and used this tool to study the localization of zinedin at cellular and subcellular levels in the rat brain. Zinedin is primarily expressed in neurons of the hippocampus, cerebral cortex, olfactory bulb and caudate putamen nucleus. Like other members of the striatin family, zinedin displays a polarized distribution in the somato-dendritic compartment of neurons and is enriched in dendritic spines. The rostral expression of zinedin as well as its compartmented distribution in dendritic spines may have important implications not only for zinedin function but also in the physiology of dendritic spines of a particular subset of neurons.

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Expression and distribution of phocein and members of the striatin family in neurones of rat peripheral ganglia

Cited by 13 publications

References 18 publications

Targeting of Proteins of the Striatin Family to Dendritic Spines: Role of the Coiled‐Coil Domain

Targeting of Proteins of the Striatin Family to Dendritic Spines: Role of the Coiled‐Coil Domain

Immunogold localization of phocein in dendritic spines

Distribution of zinedin in the rat brain

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