Clathrin’s life beyond 40: Connecting biochemistry with physiology and disease

Briant, Kit; Redlingshöfer, Lisa; Brodsky, Frances M.

doi:10.1016/j.ceb.2020.06.004

Cited by 30 publications

(35 citation statements)

References 80 publications

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“…Clathrin is a complex built of light and heavy chains that forms a coat surrounding the emerging vesicle [46]. Clathrin is required at the Golgi for vesicular transport to endosomes (for cargos such as CPY) and in endocytosis [47,48], which are Vps13-dependent processes. As shown in Figure 1a, Vps13-GFP localized to internal punctate structures, some of which contained clathrin heavy chain (Chc1) protein tagged with mCherry, Chc1-mCherry.…”

Section: Vps13 Co-localizes With Clathrin Heavy Chain Protein and Influences The Number Of Clathrin Spotsmentioning

confidence: 99%

The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi Apparatus

Kolakowski

Rzepnikowska

Kaniak-Golik

et al. 2021

IJMS

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VPS13 proteins are evolutionarily conserved. Mutations in the four human genes (VPS13A-D) encoding VPS13A-D proteins are linked to developmental or neurodegenerative diseases. The relationship between the specific localization of individual VPS13 proteins, their molecular functions, and the pathology of these diseases is unknown. Here we used a yeast model to establish the determinants of Vps13′s interaction with the membranes of Golgi apparatus. We analyzed the different phenotypes of the arf1-3 arf2Δ vps13∆ strain, with reduced activity of the Arf1 GTPase, the master regulator of Golgi function and entirely devoid of Vps13. Our analysis led us to propose that Vps13 and Arf1 proteins cooperate at the Golgi apparatus. We showed that Vps13 binds to the Arf1 GTPase through its C-terminal Pleckstrin homology (PH)-like domain. This domain also interacts with phosphoinositol 4,5-bisphosphate as it was bound to liposomes enriched with this lipid. The homologous domain of VPS13A exhibited the same behavior. Furthermore, a fusion of the PH-like domain of Vps13 to green fluorescent protein was localized to Golgi structures in an Arf1-dependent manner. These results suggest that the PH-like domains and Arf1 are determinants of the localization of VPS13 proteins to the Golgi apparatus in yeast and humans.

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Section: Vps13 Co-localizes With Clathrin Heavy Chain Protein and Influences The Number Of Clathrin Spotsmentioning

confidence: 99%

The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi Apparatus

Kolakowski

Rzepnikowska

Kaniak-Golik

et al. 2021

IJMS

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“…Engulfment into clathrin-coated vesicles is the most common and probably best studied way of receptor internalization and involves the recruitment of clathrin to heterotrimeric adaptor protein (AP) complexes. The reader is referred to recent reviews for further details ( Le Roy and Wrana, 2005 ; Edeling et al, 2006 ; Briant et al, 2020 ; Homma et al, 2021 ). Four different adaptor protein complexes AP1-AP4 that promote formation of clathrin-coated vesicles were identified.…”

Section: The Life-cycle Of Il-6 Family Receptor Complexesmentioning

confidence: 99%

“…It initially binds to membrane sites with accumulated phosphatidylinositol (4,5)-bisphosphate (PIP 2 ) at the inner leaflet of the membrane ( Figure 3A ) which leads to a conformational change exposing the cargo binding site ( Owen et al, 2004 ; Edeling et al, 2006 ). PIP 2 also promotes binding of the GTPase dynamin to the plasma membrane that catalyzes pinching off of the endocytic vesicles ( Briant et al, 2020 ).…”

Section: The Life-cycle Of Il-6 Family Receptor Complexesmentioning

confidence: 99%

Endosomes as Signaling Platforms for IL-6 Family Cytokine Receptors

Schmidt-Arras

Rose–John

2021

Front. Cell Dev. Biol.

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Interleukin-6 (IL-6) is the name-giving cytokine of a family of eleven members, including IL-6, CNTF, LIF, and IL-27. IL-6 was first recognized as a B-cell stimulating factor but we now know that the cytokine plays a pivotal role in the orchestration of inflammatory processes as well as in inflammation associated cancer. Moreover, IL-6 is involved in metabolic regulation and it has been shown to be involved in major neural activities such as neuroprotection, which can help to repair and to reduce brain damage. Receptor complexes of all members formed at the plasma membrane contain one or two molecules of the signaling receptor subunit GP130 and the mechanisms of signal transduction are well understood. IL-6 type cytokines can also signal from endomembranes, in particular the endosome, and situations have been reported in which endocytosis of receptor complexes are a prerequisite of intracellular signaling. Moreover, pathogenic GP130 variants were shown to interfere with spatial activation of downstream signals. We here summarize the molecular mechanisms underlying spatial regulation of IL-6 family cytokine signaling and discuss its relevance for pathogenic processes.

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“…Vesicle coats that initiate the budding process and direct each vesicle to its destination are most often comprised of multiple subunits (Dell'Angelica and Bonifacino, 2019;McMahon and Mills, 2004). We specifically examined the potential contribution to typhoid toxin packaging of four well-characterized coat or adaptor proteins: clathrin (Briant et al, 2020 ), coat protein complex II (COPII) (McCaughey and Stephens, 2018), and adaptor related protein complex 3 (AP3) and 4 (AP4) (Hirst et al, 2013;Odorizzi et al, 1998). We focused on these coat proteins because they carry out their function at distinct compartments within the secretory pathway.…”

Section: Copii Mediates the Formation Of Typhoid Toxin Export Carriersmentioning

confidence: 99%

Typhoid toxin sorting and exocytic transport fromSalmonellaTyphi infected cells

Chang

Lin

Lara‐Tejero

et al. 2021

Preprint

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Typhoid toxin is an essential virulence factor for Salmonella Typhi, the cause of typhoid fever in humans. This toxin has an unusual biology in that it is produced by Salmonella Typhi only when located within host cells. Once synthesized, the toxin is secreted to the lumen of the Salmonella-containing vacuole from where it is transported to the extracellular space by vesicle carrier intermediates. Here we report the identification of the typhoid toxin sorting receptor and the cellular machinery that packages the toxin into vesicle carriers, and exports it to the extracellular space. We found that the cation-independent mannose-6-phosphate receptor serves as typhoid toxin sorting receptor and that the coat protein COPII and the GTPase Sar1 mediate its packaging into vesicle carriers. Formation of the typhoid toxin carriers requires the specific environment of the Salmonella Typhi-containing vacuole, which is determined by the activities of specific effectors of its type III protein secretion systems. We also found that Rab11B and its interacting protein Rip11 control the intracellular transport of the typhoid toxin carriers, and the SNARE proteins VAMP7, SNAP23, and Syntaxin 4 their fusion to the plasma membrane. Typhoid toxin's cooption of specific cellular machinery for its transport to the extracellular space illustrates the remarkable adaptation of an exotoxin to exert its function in the context of an intracellular pathogen.

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Clathrin’s life beyond 40: Connecting biochemistry with physiology and disease

Cited by 30 publications

References 80 publications

The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi Apparatus

The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi Apparatus

Endosomes as Signaling Platforms for IL-6 Family Cytokine Receptors

Typhoid toxin sorting and exocytic transport fromSalmonellaTyphi infected cells

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