MYADM regulates Rac1 targeting to ordered membranes required for cell spreading and migration

Author:

Aranda Juan F.1,Reglero-Real Natalia1,Kremer Leonor2,Marcos-Ramiro Beatriz1,Ruiz-Sáenz Ana1,Calvo María3,Enrich Carlos4,Correas Isabel1,Millán Jaime1,Alonso Miguel A.1

Affiliation:

1. Centro de Biología Molecular Severo Ochoa, Cantoblanco, 28049 Madrid, Spain

2. Centro Nacional de Biotecnología Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain

3. Unidad de Microscopía Confocal Servicios Científico-técnicos, Facultat de Medicina Universidad de Barcelona, 08036 Barcelona, Spain

4. Departament de Biologia Celular Immunologia i Neurociències, Institut d’Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Facultat de Medicina Universidad de Barcelona, 08036 Barcelona, Spain

Abstract

Membrane organization into condensed domains or rafts provides molecular platforms for selective recruitment of proteins. Cell migration is a general process that requires spatiotemporal targeting of Rac1 to membrane rafts. The protein machinery responsible for making rafts competent to recruit Rac1 remains elusive. Some members of the MAL family of proteins are involved in specialized processes dependent on this type of membrane. Because condensed membrane domains are a general feature of the plasma membrane of all mammalian cells, we hypothesized that MAL family members with ubiquitous expression and plasma membrane distribution could be involved in the organization of membranes for cell migration. We show that myeloid-associated differentiation marker (MYADM), a protein with unique features within the MAL family, colocalizes with Rac1 in membrane protrusions at the cell surface and distributes in condensed membranes. MYADM knockdown (KD) cells had altered membrane condensation and showed deficient incorporation of Rac1 to membrane raft fractions and, similar to Rac1 KD cells, exhibited reduced cell spreading and migration. Results of rescue-of-function experiments by expression of MYADM or active Rac1L61 in cells knocked down for Rac1 or MYADM, respectively, are consistent with the idea that MYADM and Rac1 act on parallel pathways that lead to similar functional outcomes.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

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