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Golgi localisation of GMAP210 requires two distinct cis-membrane binding mechanisms by Jesus Cardenas; Sabrina Rivero; Bruno Goud; Michel Bornens; Rosa M Rios is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract ## Background The Golgi apparatus in mammals appears as a ribbon made up of interconnected stacks of flattened cisternae that is positioned close to the centrosome in a microtubule-dependent manner. How this organisation is achieved and retained is not well understood. GMAP210 is a long coiled-coil cis-Golgi associated protein that plays a role in maintaining Golgi ribbon integrity and position and contributes to the formation of the primary cilium. An amphipathic alpha-helix able to bind liposomes __in vitro__ has been recently identified at the first 38 amino acids of the protein (amphipathic lipid-packing sensor motif), and an ARF1-binding domain (Grip-related Arf-binding domain) was found at the C-terminus. To which type of membranes these two GMAP210 regions bind __in vivo__ and how this contributes to GMAP210 localisation and function remains to be investigated. ## Results By using truncated as well as chimeric mutants and videomicroscopy we found that both the N-terminus and the C-terminus of GMAP210 are targeted to the cis-Golgi __in vivo__. The ALPS motif was identified as the N-terminal binding motif and appeared concentrated in the periphery of Golgi elements

Who reads Golgi localisation of GMAP210 requires two distinct cis-membrane binding mechanisms?

Author

Jesus Cardenas; Sabrina Rivero; Bruno Goud; Michel Bornens; Rosa M Rios

Publisher

BioMed Central; Springer (Biomed Central Ltd.); [London]: BioMed Central, c2003-; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc.; Research Square (ISSN 1741-7007)

Published

2009

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)