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    RTN1 reticulon 1 [ Homo sapiens (human) ]

    Gene ID: 6252, updated on 12-Oct-2019

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Study findings show that RTN1A is a marker for cells of the dendritic lineage, including Langerhans cells and dermal dendritic cells.

    The Reticulum-Associated Protein RTN1A Specifically Identifies Human Dendritic Cells.
    Gschwandtner M, Kienzl P, Tajpara P, Schuster C, Stipek G, Buchberger M, Mildner M, Mairhofer M, Eppel W, Vierhapper M, Pammer J, Koller R, Elbe-Bürger A, Tschachler E.

    Results show that mice deficient in RTN1 are generally normal and that RTN1 is a predominantly expressed in the nervous system, mainly in neurons. In neurons, RTN1 is enriched in dendrites. Also, RTN1 deficiency shows no obvious effects on BACE1 activity due to compensation by RTN3, as RTN1 deficiency causes elevation of RTN3 expression suggesting that RTN1 does not have a prominent role in Alzheimer's pathogenesis.

    RTN1 and RTN3 protein are differentially associated with senile plaques in Alzheimer's brains.
    Shi Q, Ge Y, He W, Hu X, Yan R., Free PMC Article

    Data suggest that reticulon 1A (RTN1A) functions not only as an endoplasmic reticulum-shaping protein but also as a protein that promotes contacts between endoplasmic reticulum and mitochondria.

    Ascorbate peroxidase proximity labeling coupled with biochemical fractionation identifies promoters of endoplasmic reticulum-mitochondrial contacts.
    Cho IT, Adelmant G, Lim Y, Marto JA, Cho G, Golden JA., Free PMC Article

    Results suggest evidence of genetic association between common variants in RTN1 and end-stage kidney disease in African-Americans and European-Americans.

    Association Analysis of the Reticulon 1 Gene in End-Stage Kidney Disease.
    Bonomo JA, Palmer ND, He JC, Fan Y, Hicks PJ, Lea JP, Okusa MD, Bowden DW, Freedman BI., Free PMC Article

    RTN1A is a key mediator for proteinuria-induced tubular cell toxicity and renal fibrosis.

    Knockdown of RTN1A attenuates ER stress and kidney injury in albumin overload-induced nephropathy.
    Xiao W, Fan Y, Wang N, Chuang PY, Lee K, He JC.,

    RTN1A contributes to progression of kidney disease by inducing ER stress.

    RTN1 mediates progression of kidney disease by inducing ER stress.
    Fan Y, Xiao W, Li Z, Li X, Chuang PY, Jim B, Zhang W, Wei C, Wang N, Jia W, Xiong H, Lee K, He JC., Free PMC Article

    MANF is a protein that interacts with RTN1-C

    Identification of MANF as a protein interacting with RTN1-C.
    Chen L, Wan L, Du J, Shen Y.

    RTN-1C involvement in the regulation of Endoplasmic reticulum-mitochondria cross-talk, defines a role for RTN-1C in maintaining the function of contacts between the two organelles.

    Reticulon protein-1C is a key component of MAMs.
    Reali V, Mehdawy B, Nardacci R, Filomeni G, Risuglia A, Rossin F, Antonioli M, Marsella C, Fimia GM, Piacentini M, Di Sano F.

    RTN1-C induces PDI redistribution in endoplasmic reticulum vesicles, and concomitantly modulates its activity by decreasing the levels of its S-nitrosylated form.

    Reticulon1-C modulates protein disulphide isomerase function.
    Bernardoni P, Fazi B, Costanzi A, Nardacci R, Montagna C, Filomeni G, Ciriolo MR, Piacentini M, Di Sano F., Free PMC Article

    In the present study a potential metal ion binding motif (HxE/D) at the C-terminal of the RTN1-C has been identified and its capability to bind metals investigated by UV-vis, CD, multidimensional NMR spectroscopy and biological assays.

    A metal-binding site in the RTN1-C protein: new perspectives on the physiological role of a neuronal protein.
    Nepravishta R, Polizio F, Paci M, Melino S.

    RTN-1C is able to specifically regulate gene expression, modulating transcript clusters which have been implicated in the onset of neurodegenerative disorders

    Characterization of gene expression induced by RTN-1C in human neuroblastoma cells and in mouse brain.
    Fazi B, Biancolella M, Mehdawy B, Corazzari M, Minella D, Blandini F, Moreno S, Nardacci R, Nisticò R, Sepe S, Novelli G, Piacentini M, Di Sano F.

    Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article

    RTN-1C protein binds to DNA and that its biological function is regulated by acetylation and is coupled to the inhibition of HDAC activity.

    Acetylation of RTN-1C regulates the induction of ER stress by the inhibition of HDAC activity in neuroectodermal tumors.
    Fazi B, Melino S, De Rubeis S, Bagni C, Paci M, Piacentini M, Di Sano F.

    Nucleic acid binding of the RTN1-C C terminal region is reported with a view towards the functional role of a reticulon protein.

    Nucleic acid binding of the RTN1-C C-terminal region: toward the functional role of a reticulon protein.
    Melino S, Nepravishta R, Bellomaria A, Di Marco S, Paci M.

    analyzed the endoplasmic reticulum (ER) localization signal of human RTN1-A. Mutant proteins lacking the first (39 residues) or second (36 residues) hydrophobic segment showed ER localization

    Two hydrophobic segments of the RTN1 family determine the ER localization and retention.
    Iwahashi J, Hamada N, Watanabe H.

    These data indicate that RTN-1C is able to modulate the cellular sensitivity to different apoptotic pathways representing a promising molecular target for new drug development.

    Reticulon-1C acts as a molecular switch between endoplasmic reticulum stress and genotoxic cell death pathway in human neuroblastoma cells.
    Di Sano F, Fazi B, Tufi R, Nardacci R, Piacentini M.

    RTN1-A and RTN1-B share N-terminal 168 amino acid region, suggesting that the 168 amino acid region might play a role in regulating the endocytic process

    Human reticulon 1-A and 1-B interact with a medium chain of the AP-2 adaptor complex.
    Iwahashi J, Hamada N.

    Data demonstrate that reticulon 1 interacts specifically with spastin.

    Spastin, the most commonly mutated protein in hereditary spastic paraplegia interacts with Reticulon 1 an endoplasmic reticulum protein.
    Mannan AU, Boehm J, Sauter SM, Rauber A, Byrne PC, Neesen J, Engel W.

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