MARCH-III Is a Novel Component of Endosomes with Properties Similar to Those of MARCH-II

Fukuda, Hidekazu; Nakamura, Nobuhiro; Hirose, Shigehisa

doi:10.1093/jb/mvj012

Cited by 43 publications

(41 citation statements)

References 36 publications

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“…The E3 ubiquitin ligase MARCH II is a direct interactor that together with the related MARCH III protein regulates Stx6 distribution (13,14). Overexpression of MARCH II redistributes Stx6 to peripheral puncta that are most likely endosomes, and which contain the SNARE partner Vti1a (13).…”

Section: Discussionmentioning

confidence: 99%

“…In addition, the Habc domain of Tlg1p (the yeast orthologue of Stx6) binds to Vps51p, a component of the Vps-fifty-three (VFT)/Golgiassociated retrograde protein (GARP) tethering complex that mediates trafficking from endosomes to the late Golgi (9)(10)(11). Many binding partners for Stx6 have been identified, including the tethering factor early endosome autoantigen 1 (EEA1) (12), the RING finger E3 ubiquitin ligases MARCH II (13) and MARCH III (14), and FIG (fused in glioblastoma, also known as PIST (PDZ domain protein interacting specifically with TC10), CAL (CFTR associated ligand), GOPC (golgi-associated PDZ and coiled-coil motif containing) (15)(16)(17)(18). Most recently, GARP subunits have been shown to bind both the SNARE domain and the N-terminal domain (1-176) containing both the Habc and linker domains of Stx6 (19).…”

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confidence: 99%

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A Novel Syntaxin 6-Interacting Protein, SHIP164, Regulates Syntaxin 6-Dependent Sorting from Early Endosomes

Otto

Razi

Morvan

et al. 2010

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Membrane trafficking between organelles in eukaryotic cells is mediated by vesicular intermediates that bud from one compartment and fuse with a target compartment. Trafficking can be envisaged as sequential vesicle budding, transport, tethering and fusion reactions. SNARE proteins play an essential role in most membrane fusion reactions in eukaryotic cells, but additional factors provide the specificity of SNARE complex formation that maintains organelle identity (1), making studies of SNARE-binding proteins important. SNAREs regulate tether recruitment (2), so they may even contribute to the fidelity of membrane trafficking or enhance coordination between different trafficking steps. The bestestablished role for SNAREs is in membrane fusion, and involves formation of a four-helix bundle (or SNAREpin) between the C-terminal coiled-coil (the SNARE motif) of SNAREs on opposing membranes, bringing the two membranes into close proximity for fusion. The SNAREs are classified into two main groups based on the presence of a glutamine (Q SNAREs or t-SNAREs) or an arginine (R SNAREs or v-SNAREs) in the center of the SNARE motif (3), and all functional SNARE complexes are composed of three Q SNAREs (Qa, Qb and Qc) and one R SNARE.Many, if not all, Qa SNAREs contain a three-helix bundle at the N-terminus, called the Habc domain, which appears to have disparate functions in different SNAREs. Habc domains can regulate SNARE complex formation by intramolecular interactions with the SNARE motif (the 'closed conformation'), or can function to recruit accessory factors required for vesicle targeting, tethering or other functions. Sec1/Munc18 (SM) proteins are important binding partners of SNAREs that function at many stages of vesicle trafficking and fusion (reviewed in 4). In the case of the exocytic Qa SNARE Syntaxin 1A (Stx1A), the SM protein Munc18-1 interacts with Stx1A via at least three confirmed binding modes; Munc18-1 can bind the 'closed conformation' of Stx1A, to the N-terminus of Stx1A, and also with the assembled SNARE complex in an 'open conformation' (where the Habc domain does not interact with the SNARE motif). There is uncertainty about the exact nature of these interaction modes, with suggestions that some of the interactions involve low-affinity binding of the SM protein to a peptide that is N-terminal of the Stx1A Habc domain (5), whereas others have found that binding to the N-terminal peptide is not required for the closed conformation interaction (5). On the other hand, the interaction of the yeast SM protein Vps45p with the yeast orthologue of Stx16, Tlg2p, is largely independent of the Habc domain. Instead, Vps45p binds to an N-terminal peptide of Tlg2p, or alternatively, it can bind to the Tlg2p-SNARE complex (6).The Qc SNARE Stx6 lacks the peptide that is N-terminal to the Habc domain, and the Habc domain displays no detectable binding to the SNARE motif (7). However, it is becoming clearer that the Habc domains of the 'light chain' Qb and Qc SNARES are important for interaction with 688 www.traffic.dk

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

A Novel Syntaxin 6-Interacting Protein, SHIP164, Regulates Syntaxin 6-Dependent Sorting from Early Endosomes

Otto

Razi

Morvan

et al. 2010

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“…Thus, the MARCH10a-associated structures are likely to be microtubules. The E3 activity of several of the MARCH proteins has been shown to contribute to their subcellular localization (17,24,27). To test if the E3 activity of MARCH10a has such an effect, a mutant FLAG-MARCH10a containing serine substitutions at the conserved catalytic cysteine residues (C641S and C644S; FLAG-RINGmut) was transfected into COS7 cells, and the localization was determined by immunofluorescence microscopy.…”

Section: Super-resolution Imaging Of March10 Localization With Three-mentioning

confidence: 99%

“…Transmembrane MARCH proteins mediate the ubiquitination and subsequent down-regulation of cell-surface immune regulatory molecules, such as major histocompatibility complex class II and CD86 (17,18,21). Other proposed functions include endoplasmic reticulum-associated degradation (22), endosomal protein trafficking (23,24), mitochondrial dynamics (25,26), and spermatogenesis (19). MARCH7 (also known as Axotrophin) and MARCH10 are predicted to have no transmembrane spanning region.…”

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confidence: 99%

Membrane-associated RING-CH 10 (MARCH10 Protein) Is a Microtubule-associated E3 Ubiquitin Ligase of the Spermatid Flagella

Iyengar

Hirota

Hirose

et al. 2011

Journal of Biological Chemistry

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Background:The mechanism underlying sperm flagellar development is unknown. Results: Mammalian MARCH10 is a microtubule-associated E3 ubiquitin ligase expressed in the tail of developing spermatids. Conclusion: MARCH10 is suggested to have a role in the organization and maintenance of the sperm flagella. Significance: This is additional evidence for the involvement of the ubiquitin-proteasome system in mammalian spermatogenesis.

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“…Particularly, ubiquitination of major histocompatibility complex class I leads to its endocytosis and subsequent sorting to the MVB pathway for lysosomal degradation (18). Previously we have demonstrated that MARCH-II and -III are endosomal proteins bound to the SNARE protein syntaxin 6 and are involved in the regulation of endosomal trafficking (24,25). Hence, it is conceivable that the MARCH family could function in protein sorting and transport.…”

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confidence: 99%

MARCH-XI, a Novel Transmembrane Ubiquitin Ligase Implicated in Ubiquitin-dependent Protein Sorting in Developing Spermatids

Morokuma

Nakamura

Kato

et al. 2007

Journal of Biological Chemistry

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A mechanism by which ubiquitinated cargo proteins are sorted into multivesicular bodies (MVBs) from plasma and trans-Golgi network (TGN) membranes is well established in yeast and mammalian somatic cells. However, the ubiquitin-dependent sorting pathway has not been clearly defined in germ cells. In this study we identified a novel member of the transmembrane RING-finger family of proteins, termed membraneassociated RING-CH (MARCH)-XI, that is expressed predominantly in developing spermatids and weakly in brain and pituitary. MARCH-XI possesses an E3 ubiquitin ligase activity that targets CD4 for ubiquitination. Immunoelectron microscopy of rat round spermatids showed that MARCH-XI is localized to TGN-derived vesicles and MVBs. Fluorescence staining of rat round spermatids and immunoprecipitation of rat testis demonstrated that MARCH-XI forms complexes with the adaptor protein complex-1 and with fucose-containing glycoproteins including ubiquitinated forms. Furthermore, the C-terminal region of MARCH-XI mediates its interaction with 1-adaptin and Veli through a tyrosine-based motif and a PDZ binding motif, respectively. Our data suggest that MARCH-XI acts as a ubiquitin ligase with a role in ubiquitin-mediated protein sorting in the TGN-MVB transport pathway, which may be involved in mammalian spermiogenesis.

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MARCH-III Is a Novel Component of Endosomes with Properties Similar to Those of MARCH-II

Cited by 43 publications

References 36 publications

A Novel Syntaxin 6-Interacting Protein, SHIP164, Regulates Syntaxin 6-Dependent Sorting from Early Endosomes

A Novel Syntaxin 6-Interacting Protein, SHIP164, Regulates Syntaxin 6-Dependent Sorting from Early Endosomes

Membrane-associated RING-CH 10 (MARCH10 Protein) Is a Microtubule-associated E3 Ubiquitin Ligase of the Spermatid Flagella

MARCH-XI, a Novel Transmembrane Ubiquitin Ligase Implicated in Ubiquitin-dependent Protein Sorting in Developing Spermatids

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