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fredag 26 juni 2020

SARS2 viruksen interaktioita Golgin laitteeseen golgiiniproteiineihin

GOLGIn laite ja SARS 2 interaktioproteiinit SARS2 interaktioproteiineissa mainitaan seuraavat interaktioproteiinit:

Giantin, GCP372,  GOLGB1 , golgin B1: (Sars2 nsp3)

GRASP65,  GORASP1, GOLGI Reassembly Stacking protein 11. (Sars2 nsp13)

Golgin -95, Golgin A2, GM130, GOLGA2,  (Sars2 nsp13)

GOLGA7, Golgin subfamily A member 7.  Golgin A7 (Sars2 Spike)

Golgin-160, GOLGA3, Golgin A3 (Sars2 nsp13)

GCC2,( GRIP and coiled coil domain containing 2, GCC185, GOLGI Coiled Coil protein 185( interaktioproteiini: Sars 2 CoV nsp 13

GCC1 , (GCC88, GOLGI Coiled coil protein 88 ) (Sars2 nsp 13)

WASH complex subunit 4 (Sars2 nsp 2)
 (GOLG4 ja TMF sitovat tekijöitä, jotka sitoutuvat WASH kompleksiin. )

 Muita : 
GMAP-210, TRIP-11, GOLGI- microtubule associated protein  210 kDa.



Golgin-84, Golgin5, GOLGA5, RETII, Ret fused gene 5 protein,  https://www.genecards.org/cgi-bin/carddisp.pl?gene=GOLGA5&keywords=GOLGA5

Review ARTICLE
Front. Cell Dev. Biol., 18 June 2019 | https://doi.org/10.3389/fcell.2019.00094

The Physiological Functions of the Golgin Vesicle Tethering Proteins Martin Lowe*

  • Faculty of Biology, Medicine and Health, University of Manchester, Manchester, United Kingdom

Tethering Proteins

Martin Lowe*
  • Faculty of Biology, Medicine and Health, University of Manchester, Manchester, United Kingdom
The golgins comprise a family of vesicle tethering proteins that act in a selective manner to tether transport vesicles at the Golgi apparatus. Tethering is followed by membrane fusion to complete the delivery of vesicle-bound cargo to the Golgi. Different golgins are localized to different regions of the Golgi, and their ability to selectively tether transport vesicles is important for the specificity of vesicle traffic in the secretory pathway. In recent years, our mechanistic understanding of golgin-mediated tethering has greatly improved. We are also beginning to appreciate how the loss of golgin function can impact upon physiological processes through the use of animal models and the study of human disease. These approaches have revealed that loss of a golgin causes tissue-restricted phenotypes, which can vary in severity and the cell types affected. In many cases, it is possible to attribute these phenotypes to a defect in vesicular traffic, although why certain tissues are sensitive to loss of a particular golgin is still, in most cases, unclear. Here, I will summarize recent progress in our understanding of golgins, focusing on the physiological roles of these proteins, as determined from animal models and the study of disease in humans. I will describe what these in vivo analyses have taught us, as well as highlight less understood aspects, and areas for future investigations.
Introduction
The Golgi apparatus lies at the heart of the secretory pathway, serving to modify newly synthesized cargo proteins and to sort and transport these proteins to their final destination, which may be inside or outside the cell. It is comprised of flattened membrane compartments called cisternae that are layered on top of one another to form the Golgi stack. In non-vertebrates the Golgi stacks exist as discrete entities within the cytoplasm, whereas in vertebrates the stacks are laterally connected to form a single-copy Golgi ribbon which is located adjacent to the centrosome (Figure 1). Newly synthesized cargo proteins arriving from the endoplasmic reticulum (ER) enter the Golgi apparatus at the cis-face, which in vertebrates comprises a tubulo-vesicular compartment called the cis-Golgi network (CGN). Cargo then transits the Golgi stack before arriving at the exit station of the Golgi, the trans-Golgi network (TGN), where it is sorted into carriers for delivery to its post-Golgi destination. As cargo transits the Golgi stack, numerous resident enzymes carry...

Golgins as Vesicle Tethering Proteins

https://www.frontiersin.org/files/Articles/459614/fcell-07-00094-HTML/image_m/fcell-07-00094-g002.jpg
The golgins comprise a family of Golgi-localized coiled-coil proteins with a similar topology (Munro, 2011; Witkos and Lowe, 2015). They are anchored to the Golgi membrane by their carboxy-terminus, and extend into the cytoplasm to facilitate vesicle capture, which is in most cases is mediated by the extreme amino-terminus of the protein (Cheung et al., 2015; Gillingham and Munro, 2016; Wong et al., 2017; Gillingham, 2018). In humans, there are at least 11 golgins, with varying degrees of conservation between different eukaryotes depending upon the particular golgin. The different golgins are localized to distinct regions of the Golgi apparatus, consistent with their ability to tether different vesicle types (Wong and Munro, 2014; Gillingham and Munro, 2016; Gillingham, 2018). For example, golgins localized at the cis-Golgi are competent to selectively tether vesicles arriving from the ER and intra-Golgi vesicles mediating recycling from later Golgi cisternae, whereas those at the trans-Golgi tether vesicles arriving from the endolysosomal system (Figure 2). In contrast, golgins residing within the Golgi stack are able to tether only intra-Golgi transport vesicles. Golgins therefore play a major role in dictating the specificity of vesicle traffic within the secretory pathway. In addition, the elongated nature of the golgins, coupled with their ability to tether vesicles via their membrane-distal amino-termini, giving a greater radius of capture, allows for increased efficiency of traffic. Following vesicle capture, golgins are thought to cooperate with other proteins, including Rab GTPases and multi-subunit tethering complexes such as COG and GARP, to mediate the transition from tethering to membrane fusion, which operates over a relatively short distance and is mediated by SNARE proteins (Witkos and Lowe, 2017).
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