hShroom1 links a membrane bound protein to the actin cytoskeleton

hShroom1 (hShrm1) is a member of the Apx/Shroom (Shrm) protein family and was identified from a yeast two-hybrid screen as a protein that interacts with the cytoplasmic domain of melanoma cell adhesion molecule (MCAM). The characteristic signature of the Shrm family is the presence of a unique domai...

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Bibliographic Details
Published in:Cellular and molecular life sciences : CMLS 2009-02, Vol.66 (4), p.681-696
Main Authors: Dye, D. E, Karlen, S, Rohrbach, B, Staub, O, Braathen, L. R, Eidne, K. A, Coombe, D. R
Format: Article
Language:English
Subjects:
Actins - metabolism
Alternative Splicing
Amino Acid Sequence
Animals
Apx
Biochemistry
Bioluminescence
Biomedical and Life Sciences
Biomedicine
CD146
CD146 Antigen - genetics
CD146 Antigen - metabolism
Cell adhesion & migration
Cell Biology
Cell Line
Cytoskeleton - metabolism
Energy transfer
Humans
Life Sciences
MCAM
Melanoma
Melanoma - genetics
Melanoma - metabolism
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membranes
Microfilament Proteins - genetics
Microfilament Proteins - metabolism
Molecular biology
Molecular Sequence Data
Protein Isoforms - genetics
Protein Isoforms - metabolism
Proteins
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Research Article
Shroom
Skin cancer
Two-Hybrid System Techniques
Yeasts
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Summary:hShroom1 (hShrm1) is a member of the Apx/Shroom (Shrm) protein family and was identified from a yeast two-hybrid screen as a protein that interacts with the cytoplasmic domain of melanoma cell adhesion molecule (MCAM). The characteristic signature of the Shrm family is the presence of a unique domain, ASD2 (Apx/Shroom domain 2). mRNA analysis suggests that hShrm1 is expressed in brain, heart, skeletal muscle, colon, small intestine, kidney, placenta and lung tissue, as well a variety of melanoma and other cell lines. Co-immunoprecipitation and bioluminescence resonance energy transfer (BRET) experiments indicate that hShrm1 and MCAM interact in vivo and by immunofluorescence microscopy some co-localization of these proteins is observed. hShrm1 partly co-localises with β-actin and is found in the Triton X-100 insoluble fraction of melanoma cell extracts. We propose that hShrm1 is involved in linking MCAM to the cytoskeleton.
ISSN:1420-682X
1420-9071
DOI:10.1007/s00018-009-8645-1