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Expression of a long variant of CRACR2A that belongs to the Rab GTPase protein family in endothelial cells.

Wilson LA, McKeown L, Tumova S, Li J, Beech DJ - Biochem. Biophys. Res. Commun. (2014)

Bottom Line: Unexpectedly, short interfering RNA designed to deplete CRACR2A had no effect on CRAC channels in endothelial cells but reduced the abundance of a protein with about twice the mass of CRACR2A.It made a positive contribution to endothelial tube formation.The data suggest that endothelial cells contain a long variant of CRACR2A which is an EF-hand-containing Rab protein that lacks impact on CRAC channels.

View Article: PubMed Central - PubMed

Affiliation: School of Medicine, University of Leeds, Leeds LS2 9JT, UK.

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Sequence and Rab GTPase domains of CRACR2A-L. (A) Amino acid sequence for CRAC2RA-L. Over-lined are G boxes containing consensus residues (*) which are conserved in Rab proteins. (B) Diagram indicating features of CRACR2A-L (upper) and CRACR2A (lower). The N-terminus (N) and C-terminus (C) are indicated. The numbers are the amino acid positions in the total sequence.
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f0015: Sequence and Rab GTPase domains of CRACR2A-L. (A) Amino acid sequence for CRAC2RA-L. Over-lined are G boxes containing consensus residues (*) which are conserved in Rab proteins. (B) Diagram indicating features of CRACR2A-L (upper) and CRACR2A (lower). The N-terminus (N) and C-terminus (C) are indicated. The numbers are the amino acid positions in the total sequence.

Mentions: Analysis of the distinct long C-terminus of CRACR2A-L indicated G boxes and other sequence similarities characteristic of Rab GTPases (Fig. 3). Construction of a dendrogram placed CRACR2A-L as a previously unrecognised member of the large Rab protein family (Fig. S2). It is relatively unusual amongst the Rab proteins in containing EF hands (Fig. 3), Ca2+-binding motifs that have been shown to be functional in CRACR2A [3].


Expression of a long variant of CRACR2A that belongs to the Rab GTPase protein family in endothelial cells.

Wilson LA, McKeown L, Tumova S, Li J, Beech DJ - Biochem. Biophys. Res. Commun. (2014)

Sequence and Rab GTPase domains of CRACR2A-L. (A) Amino acid sequence for CRAC2RA-L. Over-lined are G boxes containing consensus residues (*) which are conserved in Rab proteins. (B) Diagram indicating features of CRACR2A-L (upper) and CRACR2A (lower). The N-terminus (N) and C-terminus (C) are indicated. The numbers are the amino acid positions in the total sequence.
© Copyright Policy - CC BY
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4300414&req=5

f0015: Sequence and Rab GTPase domains of CRACR2A-L. (A) Amino acid sequence for CRAC2RA-L. Over-lined are G boxes containing consensus residues (*) which are conserved in Rab proteins. (B) Diagram indicating features of CRACR2A-L (upper) and CRACR2A (lower). The N-terminus (N) and C-terminus (C) are indicated. The numbers are the amino acid positions in the total sequence.
Mentions: Analysis of the distinct long C-terminus of CRACR2A-L indicated G boxes and other sequence similarities characteristic of Rab GTPases (Fig. 3). Construction of a dendrogram placed CRACR2A-L as a previously unrecognised member of the large Rab protein family (Fig. S2). It is relatively unusual amongst the Rab proteins in containing EF hands (Fig. 3), Ca2+-binding motifs that have been shown to be functional in CRACR2A [3].

Bottom Line: Unexpectedly, short interfering RNA designed to deplete CRACR2A had no effect on CRAC channels in endothelial cells but reduced the abundance of a protein with about twice the mass of CRACR2A.It made a positive contribution to endothelial tube formation.The data suggest that endothelial cells contain a long variant of CRACR2A which is an EF-hand-containing Rab protein that lacks impact on CRAC channels.

View Article: PubMed Central - PubMed

Affiliation: School of Medicine, University of Leeds, Leeds LS2 9JT, UK.

Show MeSH