Structure of Golgi Transport Proteins

Kümmel, Daniel; Reinisch, Karin M

doi:10.1101/cshperspect.a007609

Cited by 4 publications

(7 citation statements)

References 126 publications

(153 reference statements)

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“…Sequence analysis show that the coiled-coil domains of golgins are not as continuous as predicted, but are interrupted by unstructured parts that allow strong bending and kink formation [84]. This was also nicely shown for Uso1 by rotary shadowing electron microscopy (Fig.…”

Section: Function Of Coiled-coil Tethering Factors (Cct)supporting

confidence: 66%

“…Initially, COG was localized to the rims of the Golgi cisternae as well as to vesicular structures of the cis-and trans-Golgi network [84,96,115,[123][124][125]. COG is important for the retrograde intra-Golgi trafficking, but may also function as a tether in trafficking between Golgi and endosomes, and anterograde ER-to-Golgi transport [115,118,[126][127][128][129].…”

Section: Function Of Other Mtcs Than Hops (Catchr Families)mentioning

confidence: 99%

“…These can either be achieved by the same or by coiled‐coil domains of neighboring golgins. Vesicles might get close to the Golgi‐membrane by bending of the golgin‐rod[71,84]. At the Golgi, the vesicle will be released from golgins by either changes in membrane curvature after fusion[66], or by release from the Rab with the help of a GAP protein.…”

Section: Molecular Function Of Other Tethering Factorsmentioning

confidence: 99%

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Functional homologies in vesicle tethering

2015

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a b s t r a c tThe HOPS multisubunit tethering factor (MTC) is a macromolecular protein complex composed of six different subunits. It is one of the key components in the perception and subsequent fusion of multivesicular bodies and vacuoles. Electron microscopy studies indicate structural flexibility of the purified HOPS complex. Inducing higher rigidity into HOPS by biochemically modifying the complex declines the potential to mediate SNARE-driven membrane fusion. Thus, we propose that integral flexibility seems to be not only a feature, but of essential need for the function of HOPS. This review focuses on the general features of membrane tethering and fusion. For this purpose, we compare the structure and mode of action of different tethering factors to highlight their common central features and mechanisms.

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Section: Function Of Coiled-coil Tethering Factors (Cct)supporting

confidence: 66%

Section: Function Of Other Mtcs Than Hops (Catchr Families)mentioning

confidence: 99%

Section: Molecular Function Of Other Tethering Factorsmentioning

confidence: 99%

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Functional homologies in vesicle tethering

2015

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“…2 ). Furthermore, SIDT2 shows strong co-localization with golgin-97, a protein resident of the trans-Golgi network (TGN) 35 , (Supplementary Fig. 3 ).…”

Section: Resultsmentioning

confidence: 99%

A novel family of mammalian transmembrane proteins involved in cholesterol transport

Méndez-Acevedo

Valdés

Asanov

et al. 2017

Sci Rep

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Cholesterol is an essential compound in mammalian cells because it is involved in a wide range of functions, including as a key component of membranes, precursor of important molecules such as hormones, bile acids and vitamin D. The cholesterol transport across the circulatory system is a wellknown process in contrast to the intracellular cholesterol transport, which is poorly understood. Recently in our laboratory, we identified a novel protein in C. elegans involved in dietary cholesterol uptake, which we have named ChUP-1. Insillicoanalysis identified two putative orthologue candidate proteins in mammals. The proteins SIDT1 and SIDT2 share identity and conserved cholesterol binding (CRAC) domains with C. elegans ChUP-1. Both mammalian proteins are annotated as RNA transporters in databases. In the present study, we show evidence indicating that SIDT1 and SIDT2 not only do not transport RNA, but they are involved in cholesterol transport. Furthermore, we show that single point mutations directed to disrupt the CRAC domains of both proteins prevent FRET between SIDT1 and SIDT2 and the cholesterol analogue dehydroergosterol (DHE) and alter cholesterol transport.Cholesterol is an essential molecule in mammals not only for its structural function in cell membranes, where it regulates stability, fluidity, integrity and permeability 1, 2 . Cholesterol also plays a significant role as a signaling molecule in the cells and is a precursor of other important molecules such as steroid hormones, bile acids and vitamin D.Due to the properties of cholesterol, as a highly hydrophobic molecule, it needs specialized transport mechanisms such as in the circulatory system, where it is carried as a component of lipoproteins 3 . This mechanism of cholesterol transport is well known, unlike the intracellular cholesterol transport, which remains poorly understood 4-9 . Several proteins have been identified to interact directly with cholesterol 10 . The ABC transporters are one of the most studied proteins involved in specific sterol transport across the plasma membrane of cells [6][7][8] . Another example of specific uptake is the transport protein NPC1L1, which is directly involved in the uptake of free cholesterol from the luminal space of the intestine and into enterocytes [11][12][13][14][15] . Once inside the cell, the mechanisms of cholesterol transport and redistribution and the proteins involved in such tasks remain largely unidentified 8 . There have been proposed three different mechanisms to regulate the cholesterol dynamics inside the cell 5 : transport diffusion, through contact sites between adjacent membranes and cytoplasm transport using carrier proteins.Several proteins and protein domains have been identified to interact with cholesterol 10,[16][17][18][19][20][21][22][23][24][25][26][27][28] . One of such domains in proteins is the so-called cholesterol recognition/interaction amino acid Consensus (CRAC) domain 29,30 . The sequence of this motif is characterized by the presence of the following amino acids: V/L-X(...

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“…GRASP65 and GRASP55: The mammalian Golgi reassembly stacking proteins of 65 kDa (GRASP65/GORASP1) and 55 kDa (GRASP55/GORASP2) are two homologous Golgi transport proteins localized to the cis - and medial-trans cisternae, respectively [ 120 , 121 ]. GRASPs are required for the in vitro stacking of Golgi cisternae as well as Golgi ribbon formation by linking individual stacks [ 122 , 123 , 124 ].…”

Section: Membrane Trafficking Machinerymentioning

confidence: 99%

Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation

D'Souza

Sumya

Khakurel

et al. 2021

Cells

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The Golgi is the central organelle of the secretory pathway and it houses the majority of the glycosylation machinery, which includes glycosylation enzymes and sugar transporters. Correct compartmentalization of the glycosylation machinery is achieved by retrograde vesicular trafficking as the secretory cargo moves forward by cisternal maturation. The vesicular trafficking machinery which includes vesicular coats, small GTPases, tethers and SNAREs, play a major role in coordinating the Golgi trafficking thereby achieving Golgi homeostasis. Glycosylation is a template-independent process, so its fidelity heavily relies on appropriate localization of the glycosylation machinery and Golgi homeostasis. Mutations in the glycosylation enzymes, sugar transporters, Golgi ion channels and several vesicle tethering factors cause congenital disorders of glycosylation (CDG) which encompass a group of multisystem disorders with varying severities. Here, we focus on the Golgi vesicle tethering and fusion machinery, namely, multisubunit tethering complexes and SNAREs and their role in Golgi trafficking and glycosylation. This review is a comprehensive summary of all the identified CDG causing mutations of the Golgi trafficking machinery in humans.

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Structure of Golgi Transport Proteins

Cited by 4 publications

References 126 publications

Functional homologies in vesicle tethering

Functional homologies in vesicle tethering

A novel family of mammalian transmembrane proteins involved in cholesterol transport

Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation

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