The N-terminal leucine-zipper motif in PTRF/cavin-1 is essential and sufficient for its caveolae-association.
Biochem Biophys Res Commun
; 456(3): 750-6, 2015 Jan 16.
Article
in En
| MEDLINE
| ID: mdl-25514038
ABSTRACT
PTRF/cavin-1 is a protein of two lives. Its reported functions in ribosomal RNA synthesis and in caveolae formation happen in two different cellular locations nucleus vs. plasma membrane. Here, we identified that the N-terminal leucine-zipper motif in PTRF/cavin-1 was essential for the protein to be associated with caveolae in plasma membrane. It could counteract the effect of nuclear localization sequence in the molecule (AA 235-251). Deletion of this leucine-zipper motif from PTRF/cavin-1 caused the mutant to be exclusively localized in nuclei. The fusion of this leucine-zipper motif with histone 2A, which is a nuclear protein, could induce the fusion protein to be exported from nucleus. Cell migration was greatly inhibited in PTRF/cavin-1(-/-) mouse embryonic fibroblasts (MEFs). The inhibited cell motility could only be rescued by exogenous cavin-1 but not the leucine-zipper motif deleted cavin-1 mutant. Plasma membrane dynamics is an important factor in cell motility control. Our results suggested that the membrane dynamics in cell migration is affected by caveolae associated PTRF/cavin-1.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Leucine Zippers
/
RNA-Binding Proteins
/
Caveolae
/
Membrane Proteins
Type of study:
Prognostic_studies
/
Risk_factors_studies
Limits:
Animals
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
2015
Type:
Article