Dynamin is a GTPase responsible for endocytosis in the eukaryotic cell. Dynamin is part of the "dynamin superfamily", which includes classical dynamins, dynamin-like proteins, Mx proteins, OPA1, mitofusins, and GBPs. Members of the dynamin family are principally involved in the scission of newly formed vesicles from the membrane of one cellular compartment and their targeting to, and fusion with, another compartment, both at the cell surface (particularly caveolae internalization) as well as at the Golgi apparatus.[1][2][3] Dynamin family members also play a role in many processes including division of organelles,[4] cytokinesis and microbial pathogen resistance.
https://en.wikipedia.org/wiki/Dynamin
Hermansky–Pudlak syndrome 6 (HPS6), also known as ruby-eye protein homolog (Ru), is a protein that in humans is encoded by the HPS6 gene.[5]
https://en.wikipedia.org/wiki/HPS6
https://en.wikipedia.org/wiki/SYNRG
In molecular biology, caveolins are a family of integral membrane proteins that are the principal components of caveolae membranes and involved in receptor-independent endocytosis.[1][2][3] Caveolins may act as scaffolding proteins within caveolar membranes by compartmentalizing and concentrating signaling molecules. They also induce positive (inward) membrane curvature by way of oligomerization, and hairpin insertion. Various classes of signaling molecules, including G-proteinsubunits, receptor and non-receptor tyrosine kinases, endothelial nitric oxide synthase(eNOS), and small GTPases, bind Cav-1 through its 'caveolin-scaffolding domain'.
The caveolin gene family has three members in vertebrates: CAV1, CAV2, and CAV3, coding for the proteins caveolin-1, caveolin-2, and caveolin-3, respectively. All three members are membrane proteins with similar structure. Caveolin forms oligomers and associates with cholesterol and sphingolipids in certain areas of the cell membrane, leading to the formation of caveolae.
https://en.wikipedia.org/wiki/Caveolin
Synaptophysin, also known as the major synaptic vesicle protein p38, is a protein that in humans is encoded by the SYP gene.[5][6]
https://en.wikipedia.org/wiki/Synaptophysin
Synaptotagmin-9 is a protein that in humans is encoded by the SYT9gene.[5][6]
https://en.wikipedia.org/wiki/SYT9
Munc-18 (an acronym for mammalian uncoordinated-18) proteins are the mammalian homologue of UNC-18 (which was first discovered in the nematode worm C. elegans[1][2]) and are a member of the Sec1/Munc18-like (SM) protein family. Munc-18 proteins have been identified as essential components of the synaptic vesicle fusion protein complex and are crucial for the regulated exocytosis of neurons and neuroendocrine cells.[3]
https://en.wikipedia.org/wiki/Munc-18
SAR1A (mammalian name) or Sar1 (yeast name) is a protein involved in membrane trafficking. It is a monomeric small GTPase found in COPII vesicles. It regulates the assembly and disassembly of COPII coats.
[GDP]-bound Sar1 interacts with the membrane-bound exchange factor Sec12 and exchanges its bound GDP for GTP. The hydrophobic N-terminusof Sar1-GTP then locates it to the membrane, where it serves as the binding site for the Sec23/Sec24 protein coat complex. After the vesicle coat is completely assembled and the vesicle is released from the donor membrane, the Sec23 subunit promotes Sar1 GTPase activity, which triggers the disassembly of the COPII coat.
https://en.wikipedia.org/wiki/SAR1A
An integral membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins are IMPs, but not all IMPs are transmembrane proteins.[1] IMPs comprise a significant fraction of the proteins encoded in an organism's genome.[2] Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein. Such proteins can only be separated from the membranes by using detergents, nonpolar solvents, or sometimes denaturing agents.
https://en.wikipedia.org/wiki/Integral_membrane_protein
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