Limits...
Reticulon Protein-1C: A New Hope in the Treatment of Different Neuronal Diseases.

Di Sano F, Piacentini M - Int J Cell Biol (2012)

Bottom Line: Reticulons (RTNs) are a group of membrane proteins localized on the ER and known to regulate ER structure and functions.Several studies have suggested that RTNs are involved in different important cellular functions such as changes in calcium homeostasis, ER-stress-mediated cell death, and autophagy.Reticulons have also been implicated in different signaling pathways which are at the basis of the pathogenesis of several neurodegenerative diseases.

View Article: PubMed Central - PubMed

Affiliation: Department of Biology, University of Rome "Tor Vergata", Via della Ricerca Scientifica, 00133 Rome, Italy.

ABSTRACT
Reticulons (RTNs) are a group of membrane proteins localized on the ER and known to regulate ER structure and functions. Several studies have suggested that RTNs are involved in different important cellular functions such as changes in calcium homeostasis, ER-stress-mediated cell death, and autophagy. RTNs have been demonstrated to exert a cancer specific proapoptotic function via the interaction or the modulation of specific proteins. Reticulons have also been implicated in different signaling pathways which are at the basis of the pathogenesis of several neurodegenerative diseases. In this paper we discuss the accumulating evidence identifying RTN-1C protein as a promising target in the treatment of different pathologies such as cancer or neurodegenerative disorders.

No MeSH data available.


Related in: MedlinePlus

(a) Scheme showing the reticulons distribution on endoplasmic reticulum and the physical connection between nuclear envelope and ER membrane. (b) Schematic diagram of RTN-1C and histone H4 proteins showing the shared GAKRH motif. The blue aminoacids indicate the two hydrophobic segments of RTN-1C protein. The red aminoacids indicate the three positive charges in the H4 consensus motif. RTN-1C is acetylated on Lys 204.
© Copyright Policy - open-access
Related In: Results  -  Collection


getmorefigures.php?uid=PMC3368183&req=5

fig1: (a) Scheme showing the reticulons distribution on endoplasmic reticulum and the physical connection between nuclear envelope and ER membrane. (b) Schematic diagram of RTN-1C and histone H4 proteins showing the shared GAKRH motif. The blue aminoacids indicate the two hydrophobic segments of RTN-1C protein. The red aminoacids indicate the three positive charges in the H4 consensus motif. RTN-1C is acetylated on Lys 204.

Mentions: More recently it has been reported that the synthetic peptide corresponding to the C-terminal region (aa 179–208) of the human RTN-1C is able to bind DNA. The C-terminus of RTN-1C is characterized by the presence of an H4 histone consensus motif [PS000047 HISTONE_H4] (GAKRH) [44] (Figure 1), the lysine present in this consensus sequence being one of the four residues that can be acetylated and modulate the H4 histone interaction with DNA [45].


Reticulon Protein-1C: A New Hope in the Treatment of Different Neuronal Diseases.

Di Sano F, Piacentini M - Int J Cell Biol (2012)

(a) Scheme showing the reticulons distribution on endoplasmic reticulum and the physical connection between nuclear envelope and ER membrane. (b) Schematic diagram of RTN-1C and histone H4 proteins showing the shared GAKRH motif. The blue aminoacids indicate the two hydrophobic segments of RTN-1C protein. The red aminoacids indicate the three positive charges in the H4 consensus motif. RTN-1C is acetylated on Lys 204.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3368183&req=5

fig1: (a) Scheme showing the reticulons distribution on endoplasmic reticulum and the physical connection between nuclear envelope and ER membrane. (b) Schematic diagram of RTN-1C and histone H4 proteins showing the shared GAKRH motif. The blue aminoacids indicate the two hydrophobic segments of RTN-1C protein. The red aminoacids indicate the three positive charges in the H4 consensus motif. RTN-1C is acetylated on Lys 204.
Mentions: More recently it has been reported that the synthetic peptide corresponding to the C-terminal region (aa 179–208) of the human RTN-1C is able to bind DNA. The C-terminus of RTN-1C is characterized by the presence of an H4 histone consensus motif [PS000047 HISTONE_H4] (GAKRH) [44] (Figure 1), the lysine present in this consensus sequence being one of the four residues that can be acetylated and modulate the H4 histone interaction with DNA [45].

Bottom Line: Reticulons (RTNs) are a group of membrane proteins localized on the ER and known to regulate ER structure and functions.Several studies have suggested that RTNs are involved in different important cellular functions such as changes in calcium homeostasis, ER-stress-mediated cell death, and autophagy.Reticulons have also been implicated in different signaling pathways which are at the basis of the pathogenesis of several neurodegenerative diseases.

View Article: PubMed Central - PubMed

Affiliation: Department of Biology, University of Rome "Tor Vergata", Via della Ricerca Scientifica, 00133 Rome, Italy.

ABSTRACT
Reticulons (RTNs) are a group of membrane proteins localized on the ER and known to regulate ER structure and functions. Several studies have suggested that RTNs are involved in different important cellular functions such as changes in calcium homeostasis, ER-stress-mediated cell death, and autophagy. RTNs have been demonstrated to exert a cancer specific proapoptotic function via the interaction or the modulation of specific proteins. Reticulons have also been implicated in different signaling pathways which are at the basis of the pathogenesis of several neurodegenerative diseases. In this paper we discuss the accumulating evidence identifying RTN-1C protein as a promising target in the treatment of different pathologies such as cancer or neurodegenerative disorders.

No MeSH data available.


Related in: MedlinePlus