Dynamin

Introduction to Dynamin

Dynamin is a main GTPase that plays an important role in mediating different endocytic pathways. Dynamin is an approximately 95 kDa enzyme that is composed of the GTPase domain, the proline-rich domain, SRC homologous domain as well as the GTPase effect domain. Nowadays, dynamin has been divided into three types, dynamin I, II, and III, based on the difference in the recognition of lipid membrane. Among them, dynamin I is often found in neuronal cells, dynamin III is mainly expressed in the testis, dynamin II can be identified in almost all cell types. The dynamin has been treated as a key superfamily that contains a variety of proteins, such as dynamin-like proteins (DLPs), interferon-induced GTP-binding protein Mx1, and GBPs. Many reports have demonstrated that members of the dynamin superfamily are involved in the formation of supramembranous vesicles and the fusion with cell chambers. Moreover, pilot studies have indicated that dynamin is critical for many physiological processes, which including but not limited to, endocytic membrane fission and cytokinesis.

Dynamin in the Endocytosis

In the past few years, dynamin has been proven its significant role in regulating the processes of membrane remodeling in various cell types. Meanwhile, dynamin-mediated endocytosis has also been extensively studied and the data have suggested that dynamin can participate in the membrane fission reaction for the production of an endocytic vesicle. There is considerable evidence that dynamin can form a helical polymer in the neck group of budding vesicles, and its GTP hydrolysis-dependent conformational changes promote tubular membrane fission, resulting in a free endocytic vesicle. More specifically, a battery of proteins, like Eps15, and protein adapters, including AP180/CALM are used for the binding endocytic sorting motif in a specific plasma membrane. Furthermore, dynamin can rapidly accumulate around the growing pit and generates a narrow neck by using a set of actin polymerization-associated proteins.

Besides, dynamin can also interact with a series of signaling proteins or receptors, such as neurotransmitter receptors, G protein-coupled receptors, or notch receptors on the cell surface to further analyze the partnership between endocytosis and signal transduction.

Dynamin and the Nervous System

Previous studies have shown that all three dynamin isoforms can be expressed in neurons and are expected to be essential for the basic functions of the nervous system. For example, dynamin I can interact with calcineurin via a PRITIS motif, to support synaptic vesicle recycling on the nervous system. Dynamin 3 has been considered to be critical for regulating the endocytosis of neurotransmitter receptors. It can produce certain sites that circulate the AMPA receptor in the dendritic spines. In addition, recent reports have illustrated that the dysfunction or mutations of dynamin can cause several tissue-specific diseases and epilepsy.

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