The interaction between the adaptor protein APS and Enigma is involved in actin organisation
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
The interaction between the adaptor protein APS and Enigma is involved in actin organisation. / Barres, Romain; Gonzalez, Teresa; Le Marchand-Brustel, Yannick; Tanti, Jean-François.
In: Experimental Cell Research, Vol. 308, No. 2, 15.08.2005, p. 334-44.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - The interaction between the adaptor protein APS and Enigma is involved in actin organisation
AU - Barres, Romain
AU - Gonzalez, Teresa
AU - Le Marchand-Brustel, Yannick
AU - Tanti, Jean-François
PY - 2005/8/15
Y1 - 2005/8/15
N2 - APS (adaptor protein with PH and SH2 domains) is an adaptor protein phosphorylated by several tyrosine kinase receptors including the insulin receptor. To identify novel binding partners of APS, we performed yeast two-hybrid screening. We identified Enigma, a PDZ and LIM domain-containing protein that was previously shown to be associated with the actin cytoskeleton. In HEK 293 cells, Enigma interacted specifically with APS, but not with the APS-related protein SH2-B. This interaction required the NPTY motif of APS and the LIM domains of Enigma. In NIH-3T3 cells that express the insulin receptor, Enigma and APS were partially co-localised with F-actin in small ruffling structures. Insulin increased the complex formation between APS and Enigma and their co-localisation in large F-actin containing ruffles. While in NIH-3T3 and HeLa cells the co-expression of both Enigma and APS did not modify the actin cytoskeleton organisation, expression of Enigma alone led to the formation of F-actin clusters. Similar alteration in actin cytoskeleton organisation was observed in cells expressing both Enigma and APS with a mutation in the NPTY motif. These results identify Enigma as a novel APS-binding protein and suggest that the APS/Enigma complex plays a critical role in actin cytoskeleton organisation.
AB - APS (adaptor protein with PH and SH2 domains) is an adaptor protein phosphorylated by several tyrosine kinase receptors including the insulin receptor. To identify novel binding partners of APS, we performed yeast two-hybrid screening. We identified Enigma, a PDZ and LIM domain-containing protein that was previously shown to be associated with the actin cytoskeleton. In HEK 293 cells, Enigma interacted specifically with APS, but not with the APS-related protein SH2-B. This interaction required the NPTY motif of APS and the LIM domains of Enigma. In NIH-3T3 cells that express the insulin receptor, Enigma and APS were partially co-localised with F-actin in small ruffling structures. Insulin increased the complex formation between APS and Enigma and their co-localisation in large F-actin containing ruffles. While in NIH-3T3 and HeLa cells the co-expression of both Enigma and APS did not modify the actin cytoskeleton organisation, expression of Enigma alone led to the formation of F-actin clusters. Similar alteration in actin cytoskeleton organisation was observed in cells expressing both Enigma and APS with a mutation in the NPTY motif. These results identify Enigma as a novel APS-binding protein and suggest that the APS/Enigma complex plays a critical role in actin cytoskeleton organisation.
KW - Actin Cytoskeleton
KW - Actins
KW - Adaptor Proteins, Signal Transducing
KW - Amino Acid Motifs
KW - Animals
KW - Cell Differentiation
KW - Cell Surface Extensions
KW - Cytoskeletal Proteins
KW - Cytoskeleton
KW - HeLa Cells
KW - Humans
KW - Intracellular Signaling Peptides and Proteins
KW - LIM Domain Proteins
KW - Mice
KW - NIH 3T3 Cells
KW - Protein Binding
KW - Protein Structure, Tertiary
KW - Receptor, Insulin
U2 - 10.1016/j.yexcr.2005.05.008
DO - 10.1016/j.yexcr.2005.05.008
M3 - Journal article
C2 - 15946664
VL - 308
SP - 334
EP - 344
JO - Experimental Cell Research
JF - Experimental Cell Research
SN - 0014-4827
IS - 2
ER -
ID: 45577455