Abstract
Establishment of presynaptic mechanisms by proteins that regulate neurotransmitter release in the presynaptic active zone is considered a fundamental step in animal evolution. Rab3 interacting molecule-binding proteins (Rimbps) are crucial components of the presynaptic active zone and key players in calcium homeostasis. Although Rimbp involvement in these dynamics has been described in distantly related models such as fly and human, the role of this family in most invertebrates remains obscure. To fill this gap, we defined the evolutionary history of Rimbp family in animals, from sponges to mammals. We report, for the first time, the expression of the two isoforms of the unique Rimbp family member in Ciona robusta in distinct domains of the larval nervous system. We identify intronic enhancers that are able to drive expression in different nervous system territories partially corresponding to Rimbp endogenous expression. The analysis of gene expression patterns and the identification of regulatory elements of Rimbp will positively impact our understanding of this family of genes in the context of Ciona embryogenesis.
Highlights
The exocytosis of neurotransmitter-filled synaptic vesicles of nerve and muscle cells is stabilized by various homeostatic signaling systems [1,2,3,4]
We showed that Rab3-interacting molecules (RIMs)-binding proteins (Rimbps) intronic regulatory elements are able to drive expression in papilla neurons, ascending motor ganglion neurons (AMGNs), and bipolar tail neurons (BTNs)
Within the tunicate-specific database ANISEED [31], reciprocal BLASTs revealed that the previously named Bzrap gene of C. robusta was closely related to various Rimbp2/3 family genes, for this reason, it has been called Rimbp Domain analysis confirmed that Ciona Rimbp protein shared the domain organization based on FN3 repeats and Src homology 3 (SH3) (Figure S1)
Summary
The exocytosis of neurotransmitter-filled synaptic vesicles of nerve and muscle cells is stabilized by various homeostatic signaling systems [1,2,3,4]. Modulation of presynaptic neurotransmitter release relies on an evolutionarily conserved form of homeostatic plasticity in neuromuscular junctions (NMJs), occurring in many distantly-related models ranging from insects to mammals [4,5]. The presynaptic active zone contains many conserved proteins such as Rab3-interacting molecules (RIMs), RIM-binding proteins (Rimbps), Munc, ELKS’s, and α-liprins [6]. RIMs are likely to be the central organizers that mediate direct or indirect interaction with both the remaining active zone-proteins and with those contained in the synaptic vesicles [7,8]. Rimbp proteins interact with Rims and Rims and are important components of the presynaptic active zone [9,10] as effectors of the small GTPase Rab, which is central to regulate the protein composition of the active zone [11,12,13].
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