Synaptotagmin-1: A Multi-Functional Protein that Mediates Vesicle Docking, Priming, and Fusion

Najeeb Ullah; Ezzouhra El Maaiden; Md Sahab Uddin; Ghulam Md. Ashraf

doi:10.2174/1389203722666210325110231

Synaptotagmin-1: A Multi-Functional Protein that Mediates Vesicle Docking, Priming, and Fusion

Najeeb Ullah, Ezzouhra El Maaiden, Md Sahab Uddin^*, Ghulam Md. Ashraf

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

The fusion of secretory vesicles with the plasma membrane depends on the assembly of v-SNAREs (VAMP2/synaptobrevin2) and t-SNAREs (SNAP25/syntaxinl) into the SNARE complex. Vesicles go through several upstream steps, referred to as docking and priming, to gain fusion competence. The vesicular protein synaptotagmin-1 (Syt-1) is the principal Ca²⁺ sensor for fusion in several central nervous system neurons and neuroendocrine cells and part of the docking complex for secretory granules. Syt-1 binds to the acceptor complex such as synaxin1, SNAP-25 on the plasma membrane to facilitate secretory vesicle docking, and upon Ca²⁺-influx, it promotes vesicle fusion. This review assesses the role of the Syt-1 protein involved in the secretory vesicle docking, priming, and fusion.

Original language	English
Pages (from-to)	470-478
Number of pages	9
Journal	Current Protein and Peptide Science
Volume	22
Issue number	6
DOIs	https://doi.org/10.2174/1389203722666210325110231
Publication status	Published - 2021
Externally published	Yes

Keywords

Exocytosis
Fusion
Priming
Secretory vesicles
Synaptotagmin-1
Vesicle docking

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10.2174/1389203722666210325110231

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title = "Synaptotagmin-1: A Multi-Functional Protein that Mediates Vesicle Docking, Priming, and Fusion",

abstract = "The fusion of secretory vesicles with the plasma membrane depends on the assembly of v-SNAREs (VAMP2/synaptobrevin2) and t-SNAREs (SNAP25/syntaxinl) into the SNARE complex. Vesicles go through several upstream steps, referred to as docking and priming, to gain fusion competence. The vesicular protein synaptotagmin-1 (Syt-1) is the principal Ca2+ sensor for fusion in several central nervous system neurons and neuroendocrine cells and part of the docking complex for secretory granules. Syt-1 binds to the acceptor complex such as synaxin1, SNAP-25 on the plasma membrane to facilitate secretory vesicle docking, and upon Ca2+-influx, it promotes vesicle fusion. This review assesses the role of the Syt-1 protein involved in the secretory vesicle docking, priming, and fusion.",

keywords = "Exocytosis, Fusion, Priming, Secretory vesicles, Synaptotagmin-1, Vesicle docking",

author = "Najeeb Ullah and \{El Maaiden\}, Ezzouhra and Uddin, \{Md Sahab\} and \{Md. Ashraf\}, Ghulam",

note = "Publisher Copyright: {\textcopyright} 2021 Bentham Science Publishers",

year = "2021",

doi = "10.2174/1389203722666210325110231",

language = "English",

volume = "22",

pages = "470--478",

journal = "Current Protein and Peptide Science",

issn = "1389-2037",

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T2 - A Multi-Functional Protein that Mediates Vesicle Docking, Priming, and Fusion

AU - Ullah, Najeeb

AU - El Maaiden, Ezzouhra

AU - Uddin, Md Sahab

AU - Md. Ashraf, Ghulam

PY - 2021

Y1 - 2021

N2 - The fusion of secretory vesicles with the plasma membrane depends on the assembly of v-SNAREs (VAMP2/synaptobrevin2) and t-SNAREs (SNAP25/syntaxinl) into the SNARE complex. Vesicles go through several upstream steps, referred to as docking and priming, to gain fusion competence. The vesicular protein synaptotagmin-1 (Syt-1) is the principal Ca2+ sensor for fusion in several central nervous system neurons and neuroendocrine cells and part of the docking complex for secretory granules. Syt-1 binds to the acceptor complex such as synaxin1, SNAP-25 on the plasma membrane to facilitate secretory vesicle docking, and upon Ca2+-influx, it promotes vesicle fusion. This review assesses the role of the Syt-1 protein involved in the secretory vesicle docking, priming, and fusion.

AB - The fusion of secretory vesicles with the plasma membrane depends on the assembly of v-SNAREs (VAMP2/synaptobrevin2) and t-SNAREs (SNAP25/syntaxinl) into the SNARE complex. Vesicles go through several upstream steps, referred to as docking and priming, to gain fusion competence. The vesicular protein synaptotagmin-1 (Syt-1) is the principal Ca2+ sensor for fusion in several central nervous system neurons and neuroendocrine cells and part of the docking complex for secretory granules. Syt-1 binds to the acceptor complex such as synaxin1, SNAP-25 on the plasma membrane to facilitate secretory vesicle docking, and upon Ca2+-influx, it promotes vesicle fusion. This review assesses the role of the Syt-1 protein involved in the secretory vesicle docking, priming, and fusion.

KW - Exocytosis

KW - Fusion

KW - Priming

KW - Secretory vesicles

KW - Synaptotagmin-1

KW - Vesicle docking

UR - https://www.scopus.com/pages/publications/85119627863

U2 - 10.2174/1389203722666210325110231

DO - 10.2174/1389203722666210325110231

M3 - Article

C2 - 33823763

AN - SCOPUS:85119627863

SN - 1389-2037

VL - 22

SP - 470

EP - 478

JO - Current Protein and Peptide Science

JF - Current Protein and Peptide Science

IS - 6

ER -

Synaptotagmin-1: A Multi-Functional Protein that Mediates Vesicle Docking, Priming, and Fusion

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Keywords

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