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Interaction of SQSTM1 with the motor protein dynein: SQSTM1 is required for normal dynein function and trafficking.
L Calderilla-Barbosa, ML Seibenhener, Y Du, MT Diaz-Meco, J Moscat, J Yan, MW Wooten and MC Wooten
J Cell Sci 2014 Jul 11 DOI: 10.1242/jcs.152363
Here, Calderilla-Barbosa and colleagues define an interaction between the cytoplasmic dynein motor protein complex and the SQSTM1 protein (also known as p62) a key component of the machinery that removes aggregated proteins from the cell.
This work defines the binding site on SQSTM1 and is consistent with a direct interaction with the dynein intermediate chain subunit. The data suggest that the binding site for SQSTM1 on dynein could be shared with that of the histone deacetylase HDAC6. The complex interplay between these three components remains to be defined in any real depth. However, models are proposed within the paper where the dynamic interplay of HDAC6-mediated microtubule acetylation/deacetylation, SQSTM1-mediated binding of aggregated cargo, and dynein-based motility acts to control the removal of aggregated proteins from within cells.
While much of the data rely on immunofluorescence of dynein, which must always be treated with caution owing to the difficulty of detecting specific dynein immunolabelling in cells, it is clear from this work that dynein and SQSTM1 have an interdependent relationship in the removal of aggregated proteins from cells.
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