RGD Reference Report - Arl6IP1 has the ability to shape the mammalian ER membrane in a reticulon-like fashion. - Rat Genome Database

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Arl6IP1 has the ability to shape the mammalian ER membrane in a reticulon-like fashion.

Authors: Yamamoto, Y  Yoshida, A  Miyazaki, N  Iwasaki, K  Sakisaka, T 
Citation: Yamamoto Y, etal., Biochem J. 2014 Feb 15;458(1):69-79. doi: 10.1042/BJ20131186.
RGD ID: 11059584
Pubmed: PMID:24262037   (View Abstract at PubMed)
DOI: DOI:10.1042/BJ20131186   (Journal Full-text)

The ER (endoplasmic reticulum) consists of the nuclear envelope and a peripheral network of membrane sheets and tubules. Two classes of the evolutionarily conserved ER membrane proteins, reticulons and REEPs (receptor expression-enhancing proteins)/DP1 (deleted in polyposis locus 1)/Yop1 (YIP 1 partner), shape high-curvature ER tubules. In mammals, four members of the reticulon family and six members of the REEP family have been identified so far. In the present paper we report that Arl6IP1(ADP-ribosylation factor-like 6 interacting protein 1), an anti-apoptotic protein specific to multicellular organisms, is a potential player in shaping the ER tubules in mammalian cells. Arl6IP1, which does not share an overall primary sequence homology with reticulons, harbours reticulon-like short hairpin transmembrane domains and binds to atlastin, a GTPase that mediates the formation of the tubular ER network. Overexpression of Arl6IP1 induced extensive tubular structures of the ER and excluded a luminal protein. Furthermore, overexpression of Arl6IP1 stabilized the ER tubules, allowing the cells to maintain the ER tubules even in the absence of microtubules. Arl6IP1 constricted liposomes into tubules. The short hairpin structures of the transmembrane domains were required for the membrane-shaping activity of Arl6IP1. The results of the present study indicate that Arl6IP1 has the ability to shape high-curvature ER tubules in a reticulon-like fashion.




Cellular Component

  
Object Symbol
Species
Term
Qualifier
Evidence
With
Notes
Source
Original Reference(s)
VapaRatendoplasmic reticulum membrane located_inIDA PMID:24262037UniProt 
VapaRatnuclear membrane located_inIDA PMID:24262037UniProt 

Molecular Function

  
Object Symbol
Species
Term
Qualifier
Evidence
With
Notes
Source
Original Reference(s)
Atl1Ratprotein binding enablesIPIUniProtKB:Q15041PMID:24262037UniProt 


Genes (Rattus norvegicus)
Atl1  (atlastin GTPase 1) Vapa  (VAMP associated protein A)