RGD Reference Report - CLP36 and RIL recruit a-actinin-1 to stress fibers and differentially regulate stress fiber dynamics in F2408 fibroblasts. - Rat Genome Database

Send us a Message



Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   

CLP36 and RIL recruit a-actinin-1 to stress fibers and differentially regulate stress fiber dynamics in F2408 fibroblasts.

Authors: Miyazaki, Kazufumi  Ohno, Koji  Tamura, Naoaki  Sasaki, Takeshi  Sato, Kohji 
Citation: Miyazaki K, etal., Exp Cell Res. 2012 Aug 15;318(14):1716-25. doi: 10.1016/j.yexcr.2012.05.006. Epub 2012 May 30.
RGD ID: 13432282
Pubmed: PMID:22659164   (View Abstract at PubMed)
DOI: DOI:10.1016/j.yexcr.2012.05.006   (Journal Full-text)

CLP36 is a member of the ALP/Enigma protein family and has been shown to be localized to stress fibers in various cells. We previously reported that depletion of CLP36 caused loss of stress fibers in BeWo choriocarcinoma cells, but it remains unclear how CLP36 contributes to stress fiber formation. In this study, we generated CLP36-depleted F2408 fibroblasts and found that stress fibers showed abnormal non-oriented organization in these cells. In addition to CLP36, F2408 cells contained RIL, another ALP/Enigma protein, and we demonstrated that RIL could compensate for the role of CLP36 in stress fiber formation. CLP36 and RIL form a complex with α-actinin-1 and palladin. We found a strong correlation between loss of CLP36/RIL and failure of α-actinin-1 or palladin to localize on stress fibers. In addition, time lapse observation revealed that incorporation of RIL stabilizes stress fibers and that CLP36 influences the dynamic architecture of these fibers. Our findings indicate that CLP36 and RIL have a redundant role in the formation of stress fibers, but have different effects on stress fiber dynamics in F2408 cells.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Pdlim1Ratactin cytoskeleton organization involved_inIMP PMID:22659164UniProt 
Pdlim1Ratestablishment or maintenance of actin cytoskeleton polarity involved_inIMP PMID:22659164UniProt 
Pdlim1Ratfibroblast migration involved_inIMP PMID:22659164UniProt 
Pdlim1Ratmaintenance of cell polarity involved_inIMP PMID:22659164UniProt 
Pdlim4Ratpositive regulation of stress fiber assembly involved_inIMP PMID:22659164UniProt 
Pdlim1Ratstress fiber assembly involved_inIMP PMID:22659164UniProt 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Pdlim1Ratactin cytoskeleton located_inIDA PMID:22659164UniProt 
Pdlim1Ratcytoplasm located_inIDA PMID:22659164UniProt 
PalldRatstress fiber located_inIDA PMID:22659164UniProt 
Pdlim1Ratstress fiber located_inIDA PMID:22659164UniProt 
Pdlim4Ratstress fiber located_inIDA PMID:22659164UniProt 
Pdlim1RatZ disc located_inIDA PMID:22659164UniProt 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Pdlim1Ratactin binding enablesIDA PMID:22659164UniProt 
Actn1Ratprotein binding enablesIPIUniProtKB:P52944PMID:22659164UniProt 
Pdlim1Ratprotein binding enablesIPIUniProtKB:Q9Z1P2PMID:22659164UniProt 
Pdlim1Ratprotein binding enablesIPIUniProtKB:P36202PMID:22659164UniProt 
Pdlim4Ratprotein binding enablesIPIUniProtKB:P52944PMID:22659164UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Actn1  (actinin, alpha 1)
Palld  (palladin, cytoskeletal associated protein)
Pdlim1  (PDZ and LIM domain 1)
Pdlim4  (PDZ and LIM domain 4)


Additional Information