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In search for an appropriate model to study the role of MYO5B in apical membrane protein trafficking
Author(s) -
Mackovicova Katarina,
Goot Annemieke T,
Sjollema Klaas A,
Nollen Ellen AA,
Ijzendoorn Sven CD
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.506.1
Subject(s) - intracellular , microbiology and biotechnology , apical membrane , biology , brush border , membrane protein , cell polarity , endosome , cell , chemistry , membrane , biochemistry , vesicle
Recently, the mutations in MYO5B gene (encoding for actin‐binding motor protein involved in endosomal recycling to apical membrane) were associated with disturbed intracellular protein trafficking to apical membrane. We aimed to establish a model to study the involvement of MYO5B in protein trafficking. Expression of MYO5B, polarization, intracellular trafficking and microvillous ultrastructure were analyzed in 3D cultures of intestinal T84 and Caco‐2 cell lines and in the intestines of hum‐2 (orthologue of human MYO5B)‐deficient C.elegans by fluorescent and electron microscopy. In contrast to Caco‐2, T84 did not express MYO5B, but the ability of both cell lines to polarize, regulate intracellular trafficking and form microvillous brush border was intact. Similarly, hum‐2‐deficient C.elegans showed no intestinal ultrastructural changes or protein mislocalization. MYO5B deficiency alone did not provide the phenotype mimicking disturbed apical membrane protein trafficking in T84 cell line nor in C.elegans. Mechanisms additional to MYO5B malfunction might play role in altered protein trafficking to apical membrane.