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      SIP30 involvement in vesicle exocytosis from PC12 cells

      brief-report
      Author(s): , ∗
      Publication date (Electronic):
      Journal: Biochemistry and Biophysics Reports
      Publisher: Elsevier
      Keywords: SIP30, Exocytosis, Synaptic vesicles, PC12 cells, Neuropathic pain

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          Abstract

          SNAP25 (synaptosome-associated protein of 25 kDa) is a core SNARE (soluble N-ethylmaleimide-sensitive factor attachment receptor) protein; and the interaction between SNAP25 and other SNARE proteins is essential for synaptic vesicle exocytosis. Identified as a SNAP25 interacting protein, SIP30 (SNAP25 interacting protein at 30 kDa) has been shown to modulate neuropathic pain behavior, and is potentially involved in the cellular process of vesicle exocytosis. Previous study demonstrated that using a vesicle secretion assay in PC12 cells, anti-SIP30 siRNA reduced vesicle exocytosis. We investigated vesicle exocytosis from PC12 cells with FM1-43 fluorescence dye, and demonstrated that anti-SIP30 siRNA reduced the pool of releasable vesicles and the rate of vesicle exocytosis, without affecting the endocytosis and recycling of the exocytosed vesicles. The results show that SIP30 is involved in vesicle exocytosis, suggesting a potential mechanism of SIP30 modulation of neuropathic pain.

          Highlights

          • •

            SIP30 is a SNARE protein involved in neuropathic pain modulation.

          • •

            Inhibition of SIP30 in PC12 cells reduced the pool of releasable vesicles and the rate of vesicle exocytosis, without affecting the endocytosis and recycling of the exocytosed vesicles.

          • •

            This suggests SIP30 involvement in vesicle exocytosis, thereby modulating neuropathic pain.

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          Most cited references35

          • Record: found
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          Membrane fusion: grappling with SNARE and SM proteins.

          Thomas C. Südhof, James Rothman (2009)
          The two universally required components of the intracellular membrane fusion machinery, SNARE and SM (Sec1/Munc18-like) proteins, play complementary roles in fusion. Vesicular and target membrane-localized SNARE proteins zipper up into an alpha-helical bundle that pulls the two membranes tightly together to exert the force required for fusion. SM proteins, shaped like clasps, bind to trans-SNARE complexes to direct their fusogenic action. Individual fusion reactions are executed by distinct combinations of SNARE and SM proteins to ensure specificity, and are controlled by regulators that embed the SM-SNARE fusion machinery into a physiological context. This regulation is spectacularly apparent in the exquisite speed and precision of synaptic exocytosis, where synaptotagmin (the calcium-ion sensor for fusion) cooperates with complexin (the clamp activator) to control the precisely timed release of neurotransmitters that initiates synaptic transmission and underlies brain function.
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            The mechanisms and functions of spontaneous neurotransmitter release.

            Ege Kavalali (2015)
            Fast synaptic communication in the brain requires synchronous vesicle fusion that is evoked by action potential-induced Ca(2+) influx. However, synaptic terminals also release neurotransmitters by spontaneous vesicle fusion, which is independent of presynaptic action potentials. A functional role for spontaneous neurotransmitter release events in the regulation of synaptic plasticity and homeostasis, as well as the regulation of certain behaviours, has been reported. In addition, there is evidence that the presynaptic mechanisms underlying spontaneous release of neurotransmitters and their postsynaptic targets are segregated from those of evoked neurotransmission. These findings challenge current assumptions about neuronal signalling and neurotransmission, as they indicate that spontaneous neurotransmission has an autonomous role in interneuronal communication that is distinct from that of evoked release.
            Article 0 comments Cited 160 times – based on 0 reviews     Review now
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              A complete genetic analysis of neuronal Rab3 function.

              Oliver Schlüter, Frank Schmitz, Reinhard Jahn … (2004)
              Rab3A, Rab3B, Rab3C, and Rab3D are closely related GTP-binding proteins of synaptic vesicles that may function in neurotransmitter release. We have produced knock-out (KO) mice for Rab3B and Rab3C and crossed them with previously generated Rab3A and 3D knock-out mice to generate double, triple, and quadruple Rab3 knock-out mice. We have found that all single and double Rab3 knock-out mice are viable and fertile. Most triple Rab3 knock-out mice perish whenever Rab3A is one of the three deleted proteins, whereas all triple knock-out mice that express Rab3A are viable and fertile. Finally, all quadruple knock-out mice die shortly after birth. Quadruple Rab3 KO mice initially develop normally and are born alive but succumb to respiratory failure. Rab3-deficient mice display no apparent changes in synapse structure or brain composition except for a loss of rabphilin, a Rab3-binding protein. Analysis of cultured hippocampal neurons from quadruple knock-out mice uncovered no significant change in spontaneous or sucrose-evoked release but an approximately 30% decrease in evoked responses. This decrease was caused by a decline in the synaptic and the vesicular release probabilities, suggesting that Rab3 proteins are essential for the normal regulation of Ca2+-triggered synaptic vesicle exocytosis but not for synaptic vesicle exocytosis as such. Our data show that Rab3 is required for survival in mice and that the four Rab3 proteins are functionally redundant in this role. Furthermore, our data demonstrate that Rab3 is not in itself essential for synaptic membrane traffic but functions to modulate the basic release machinery.
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                Author and article information

                Contributors
                Lei Yu
                Journal
                Journal ID (nlm-ta): Biochem Biophys Rep
                Journal ID (iso-abbrev): Biochem Biophys Rep
                Title: Biochemistry and Biophysics Reports
                Publisher: Elsevier
                ISSN (Electronic): 2405-5808
                Publication date PMC-release: 15 December 2023
                Publication date Collection: March 2024
                Publication date (Electronic): 15 December 2023
                Volume: 37
                Electronic Location Identifier: 101614
                Affiliations
                [1]Department of Genetics, and Center of Alcohol & Substance Use Studies, Rutgers University, Piscataway, NJ, 08854, USA
                Author notes
                [∗ ]Corresponding author. yu@ 123456biology.rutgers.edu
                Article
                Publisher Item ID: S2405-5808(23)00195-4 Publisher ID: 101614
                DOI: 10.1016/j.bbrep.2023.101614
                PMC ID: 10770524
                PubMed ID: 38188363
                SO-VID: 9cad1178-9e9d-405c-a379-54c7f798ec4e
                Copyright © © 2023 The Authors
                License:

                This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 22 November 2023
                Date revision received : 7 December 2023
                Date accepted : 11 December 2023
                Categories
                Subject: Short Communication

                Keywords: sip30,exocytosis,synaptic vesicles,pc12 cells,neuropathic pain
                Data availability:
                Keywords: sip30, exocytosis, synaptic vesicles, pc12 cells, neuropathic pain

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