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Type F scavenger receptor SREC-I interacts with advillin, a member of the gelsolin/villin family, and induces neurite-like outgrowth.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2004 Sep 17; Vol. 279 (38), pp. 40084-90. Date of Electronic Publication: 2004 Jul 09. - Publication Year :
- 2004
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Abstract
- The scavenger receptor expressed by endothelial cells (SREC) was isolated from a human endothelial cell line and consists of two isoforms named SREC-I and -II. Both isoforms have no significant homology to other types of scavenger receptors. They contain 10 repeats of epidermal growth factor-like cysteine-rich motifs in the extracellular domains and have unusually long C-terminal cytoplasmic domains with Ser/Pro-rich regions. The extracellular domain of SREC-I binds modified low density lipoprotein and mediates a homophilic SREC-I/SREC-I or heterophilic SREC-I/SREC-II trans-interaction. However, the significance of large Ser/Pro-rich cytoplasmic domains of SRECs is not clear. Here, we found that when SREC-I was overexpressed in murine fibroblastic L cells, neurite-like outgrowth was induced, indicating that the receptor can lead to changes in cell morphology. The SREC-I-mediated morphological change required the cytoplasmic domain of the protein, and we identified advillin, a member of the gelsolin/villin family of actin regulatory proteins, as a protein binding to this domain. Reduction of advillin expression in L cells by RNAi led to the absence of the described SREC-I-induced morphological changes, indicating that advillin is a prerequisite for the change. Finally, we demonstrated that SREC-I and advillin were co-expressed and interacted with each other in dorsal root ganglion neurons during embryonic development and that overexpression of both SREC-I and advillin in cultured Neuro-2a cells induced long process formation. These results suggest that the interaction of SREC-I and advillin are involved in the development of dorsal root ganglion neurons by inducing the described morphological changes.
- Subjects :
- Amino Acid Sequence
Animals
Cell Adhesion Molecules chemistry
Cell Adhesion Molecules genetics
Cell Size physiology
Cells, Cultured
Cytoplasm metabolism
Ganglia, Spinal cytology
Gelsolin genetics
Mice
Microfilament Proteins genetics
Molecular Sequence Data
Neurons physiology
Neurons ultrastructure
Protein Structure, Tertiary
Receptors, LDL chemistry
Receptors, LDL genetics
Receptors, Scavenger
Scavenger Receptors, Class F
Transfection
Cell Adhesion Molecules metabolism
Microfilament Proteins metabolism
Neurites physiology
Receptors, LDL metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 279
- Issue :
- 38
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 15247299
- Full Text :
- https://doi.org/10.1074/jbc.M403844200