Reticulon 1‐C/neuroendocrine‐specific protein‐C interacts with SNARE proteins

Steiner, Pascal; Kulangara, Karina; Sarria, J.-C. Floyd; Glauser, Liliane; Regazzi, Romano; Hirling, Harald

doi:10.1111/j.1471-4159.2004.02345.x

Cited by 84 publications

(74 citation statements)

References 38 publications

(95 reference statements)

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“…6). An RTN family protein interacts with soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins (21) and is also involved in membrane trafficking between the endoplasmic reticulum and Golgi (22). SNAREs comprise three families of proteins: a synaptosomalassociated protein of 25 kDa (SNAP-25) and its related isoforms, the syntaxins, and vesicle-associated membrane proteins.…”

Section: Discussionmentioning

confidence: 99%

Reticulon 3 Binds the 2C Protein of Enterovirus 71 and Is Required for Viral Replication

Tang¹,

Yang²,

Wu³

et al. 2007

Journal of Biological Chemistry

137

124

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Enterovirus 71 is an enterovirus of the family Picornaviridae. The 2C protein of poliovirus, a relative of enterovirus 71, is essential for viral replication. The poliovirus 2C protein is associated with host membrane vesicles, which form viral replication complexes where viral RNA synthesis takes place. We have now identified a host-encoded 2C binding protein called reticulon 3, which we found to be associated with the replication complex through direct interaction with the enterovirus 71-encoded 2C protein. We observed that the N terminus of the 2C protein, which has both RNA-and membrane-binding activity, interacted with reticulon 3. This region of interaction was mapped to its reticulon homology domain, whereas that of 2C was encoded by the 25th amino acid, isoleucine. Reticulon 3 could also interact with the 2C proteins encoded by other enteroviruses, such as poliovirus and coxsackievirus A16, implying that it is a common factor for such viral replication. Reduced production of reticulon 3 by RNA interference markedly reduced the synthesis of enterovirus 71-encoded viral proteins and replicative doublestranded RNA, reducing plaque formation and apoptosis. Furthermore, reintroduction of nondegradable reticulon 3 into these knockdown cells rescued enterovirus 71 infectivity, and viral protein and double-stranded RNA synthesis. Thus, reticulon 3 is an important component of enterovirus 71 replication, through its potential role in modulation of the sequential interactions between enterovirus 71 viral RNA and the replication complex.

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Section: Discussionmentioning

confidence: 99%

Reticulon 3 Binds the 2C Protein of Enterovirus 71 and Is Required for Viral Replication

Tang¹,

Yang²,

Wu³

et al. 2007

Journal of Biological Chemistry

137

124

View full text Add to dashboard Cite

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“…LCR-containing proteins were shown to interact with numerous protein partners within protein interaction networks and were more often associated with hubs (Coletta et al, 2010). Particularly, mammalian RTNs were shown to bind to components of the general transport pathways, such as SNAREs (Steiner et al, 2004), and the adaptor protein complex AP2 (Iwahashi and Hamada, 2003) with roles in transport vesicle formation and recycling. It is possible that the TDMs and LCRs present in RTNLB1 and RTNLB2 offer interfaces for the interaction with protein partners necessary for regulating aspects of FLS2 transport.…”

Section: Rtnlb1 and Rtnlb2 And Their Relationship With Two Processes mentioning

confidence: 99%

Arabidopsis RTNLB1 and RTNLB2 Reticulon-Like Proteins Regulate Intracellular Trafficking and Activity of the FLS2 Immune Receptor

et al. 2011

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Receptors localized at the plasma membrane are critical for the recognition of pathogens. The molecular determinants that regulate receptor transport to the plasma membrane are poorly understood. In a screen for proteins that interact with the FLAGELIN-SENSITIVE2 (FLS2) receptor using Arabidopsis thaliana protein microarrays, we identified the reticulon-like protein RTNLB1. We showed that FLS2 interacts in vivo with both RTNLB1 and its homolog RTNLB2 and that a Ser-rich region in the N-terminal tail of RTNLB1 is critical for the interaction with FLS2. Transgenic plants that lack RTNLB1 and RTNLB2 (rtnlb1 rtnlb2) or overexpress RTNLB1 (RTNLB1ox) exhibit reduced activation of FLS2-dependent signaling and increased susceptibility to pathogens. In both rtnlb1 rtnlb2 and RTNLB1ox, FLS2 accumulation at the plasma membrane was significantly affected compared with the wild type. Transient overexpression of RTNLB1 led to FLS2 retention in the endoplasmic reticulum (ER) and affected FLS2 glycosylation but not FLS2 stability. Removal of the critical N-terminal Serrich region or either of the two Tyr-dependent sorting motifs from RTNLB1 causes partial reversion of the negative effects of excess RTNLB1 on FLS2 transport out of the ER and accumulation at the membrane. The results are consistent with a model whereby RTNLB1 and RTNLB2 regulate the transport of newly synthesized FLS2 to the plasma membrane.

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“…Correlations with such genes are indicative of a role in myogenic differentiation. Through interaction with SNARE proteins RTN1 is involved in vesicle trafficking and exocytosis, including growth hormone secretion (78). RTN1 is also potentially a nuclease and an inhibitor of histone deacetylases (48,55), a function that leads to the dissociation of histones from DNA resulting in increased transcription.…”

Section: Genes Associated With Muscle Fiber Differentiation and Positmentioning

confidence: 99%

Discovery and characterization of nutritionally regulated genes associated with muscle growth in Atlantic salmon

Bower

Johnston

2010

Physiological Genomics

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Reticulon 1‐C/neuroendocrine‐specific protein‐C interacts with SNARE proteins

Cited by 84 publications

References 38 publications

Reticulon 3 Binds the 2C Protein of Enterovirus 71 and Is Required for Viral Replication

Reticulon 3 Binds the 2C Protein of Enterovirus 71 and Is Required for Viral Replication

Arabidopsis RTNLB1 and RTNLB2 Reticulon-Like Proteins Regulate Intracellular Trafficking and Activity of the FLS2 Immune Receptor

Discovery and characterization of nutritionally regulated genes associated with muscle growth in Atlantic salmon

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