Recruitment of the Mint3 Adaptor Is Necessary for Export of the Amyloid Precursor Protein (APP) from the Golgi Complex

Caster, Amanda H.; Kahn, Richard

doi:10.1074/jbc.m113.481101

Cited by 33 publications

(32 citation statements)

References 55 publications

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“…Interestingly, although some localization of Mint3 was seen in Golgi, consistent with other reports (25), unlike other cell types, Mint3 showed a strong nuclear localization in NP cells. Furthermore, in contrast to previous findings in macrophages that showed a prominent perinuclear co-localization between Mint3 and FIH-1 (23), these proteins showed a strong nuclear staining and co-localization in NP cells.…”

Section: Discussionsupporting

confidence: 91%

FIH-1-Mint3 Axis Does Not Control HIF-1α Transcriptional Activity in Nucleus Pulposus Cells

Hirose

Johnson

Schoepflin

et al. 2014

Journal of Biological Chemistry

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Section: Discussionsupporting

confidence: 91%

FIH-1-Mint3 Axis Does Not Control HIF-1α Transcriptional Activity in Nucleus Pulposus Cells

Hirose

Johnson

Schoepflin

et al. 2014

Journal of Biological Chemistry

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“…Rab5 was found only in the crude endosomal fraction, whereas LAMP1 and EEA1 were also present in the Golgi and ER fraction. Given that LAMP1 and EEA1 participate in post-Golgi trafficking events, these observations were not entirely surprising (Caster and Kahn, 2013;Luo et al, 2006).…”

Section: Psmc5 and Shoc2 Colocalize On Late Endosomes And/or Mvbsmentioning

confidence: 95%

Spatial control of Shoc2 scaffold-mediated ERK1/2 signaling requires remodeling activity of the ATPase PSMC5

Jang

Shi

et al. 2015

Journal of Cell Science

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The scaffold protein Shoc2 accelerates activity of the ERK1 and ERK2 (ERK1/2, also known as MAPK3 and MAPK1) pathway. Mutations in Shoc2 result in Noonan-like RASopathy, a developmental disorder with a wide spectrum of symptoms. The amplitude of the ERK1/2 signals transduced through the complex is fine-tuned by the HUWE1-mediated ubiquitylation of Shoc2 and its signaling partner RAF-1. Here, we provide a mechanistic basis of how ubiquitylation of Shoc2 and RAF-1 is controlled. We demonstrate that the newly identified binding partner of Shoc2, the (AAA+) ATPase PSMC5, triggers translocation of Shoc2 to endosomes. At the endosomes, PSMC5 displaces the E3 ligase HUWE1 from the scaffolding complex to attenuate ubiquitylation of Shoc2 and RAF-1. We show that a RASopathy mutation that changes the subcellular distribution of Shoc2 leads to alterations in Shoc2 ubiquitylation due to the loss of accessibility to PSMC5. In summary, our results demonstrate that PSMC5 is a new and important player involved in regulating ERK1/2 signal transmission through the remodeling of Shoc2 scaffold complex in a spatially-defined manner.

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“…Thus, retention of TRAF3 at the ER-to-Golgi vesicular transport system blunted the ability of TRAF3 to interact with MAVS upon viral infection and consequently decreased type I IFN secretion (15). Mint3 associates with several membrane proteins in Golgi and regulate their traffic from the trans-Golgi network (10)(11)(12). We found that Mint3 deficiency dramatically changed the TRAF3 distribution from a speckle pattern to a diffuse pattern.…”

Section: Discussionmentioning

confidence: 83%

“…Mint3 was originally identified as an Alzheimer disease β-amyloid precursor protein (APP) interactor (9). Mint3 associates with several membrane proteins such as APP and furin in Golgi and regulates the traffic of these proteins from the trans-Golgi network (10)(11)(12). Mint3 regulates ATP production in macrophages and augments LPS-induced septic shock by enhancing the activity of hypoxia-inducible factor-1 (13,14).…”

mentioning

confidence: 99%

Mint3 potentiates TLR3/4- and RIG-I–induced IFN-β expression and antiviral immune responses

Huai

Song

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Type I IFNs (IFN-α/β) play crucial roles in the elimination of invading viruses. Multiple immune cells including macrophages recognize viral infection through a variety of pattern recognition receptors, such as Toll-like receptors (TLRs) and retinoic acid-inducible gene-I (RIG-I)-like receptors, and initiate type I IFN secretion and subsequent antiviral immune responses. However, the mechanisms by which host immune cells can produce adequate amounts of type I IFNs and then eliminate viruses effectively remain to be further elucidated. In the present study, we show that munc18-1-interacting protein 3 (Mint3) expression can be markedly induced during viral infection in macrophages. Mint3 enhances TLR3/4-and RIG-I-induced IRF3 activation and IFN-β production by promoting K63-linked polyubiquitination of TNF receptor-associated factor 3 (TRAF3). Consistently, Mint3 deficiency greatly attenuated antiviral immune responses and increased viral replication. Therefore, we have identified Mint3 as a physiological positive regulator of TLR3/4 and RIG-I-induced IFN-β production and have outlined a feedback mechanism for the control of antiviral immune responses.interferon | viral infection | TLR | RIG-I | TRAF3

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Recruitment of the Mint3 Adaptor Is Necessary for Export of the Amyloid Precursor Protein (APP) from the Golgi Complex

Abstract: Background: Traffic of the amyloid precursor protein (APP) determines its processing to neurotoxic A␤ peptides. Results: Mint3 is recruited to the Golgi by APP and is required for export to a LAMP1 ϩ compartment.

Cited by 33 publications

References 55 publications

FIH-1-Mint3 Axis Does Not Control HIF-1α Transcriptional Activity in Nucleus Pulposus Cells

FIH-1-Mint3 Axis Does Not Control HIF-1α Transcriptional Activity in Nucleus Pulposus Cells

Spatial control of Shoc2 scaffold-mediated ERK1/2 signaling requires remodeling activity of the ATPase PSMC5

Mint3 potentiates TLR3/4- and RIG-I–induced IFN-β expression and antiviral immune responses

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