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

Aranda, Juan; Reglero-Real, Natalia; Kremer, Leonor; Marcos‐Ramiro, Beatriz; Ruiz-Sáenz, Ana; Calvo, Marı́a; Enrich, Carlos; Correas, Isabel; Millán, Jaime; Alonso, Miguel A.

doi:10.1091/mbc.e10-11-0910

Cited by 46 publications

(55 citation statements)

References 48 publications

(104 reference statements)

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“…Thus, the known structure of tetherin provides an explanation for its capacity to serve as an organiser of lipid rafts and it joins a growing number of proteins [e.g. tetraspanins, annexins, galectins, caveolins, cavins, flotillins, MYADM (Aranda et al, 2011;Claas et al, 2001;Frick et al, 2007;Grewal et al, 2010;Hill et al, 2008;Lajoie et al, 2009;Stuermer et al, 2001)] that perform roles in the organisation of membrane microdomains.…”

Section: Discussionmentioning

confidence: 99%

CD317/Tetherin is an organiser of membrane microdomains

Billcliff

Rollason

Prior

et al. 2013

Journal of Cell Science

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SummaryThe integral membrane protein tetherin has been associated with an eclectic mix of cellular processes, including restricting the release of a range of enveloped viruses from infected cells. The unusual topology of tetherin (it possesses both a conventional transmembrane domain and a glycosylphosphatidylinositol anchor), its localisation to membrane microdomains (lipid rafts) and the fact that its cytosolic domain can be linked (indirectly) to the actin cytoskeleton, led us to speculate that tetherin might form a 'tethered picket fence' and thereby play a role in the organisation of lipid rafts. We now show that knocking down expression of tetherin leads to changes in the distribution of lipid raft-localised proteins and changes in the organisation of lipids in the plasma membrane. These changes can be reversed by re-expression of wild-type tetherin, but not by any of a range of tetherin-based constructs, indicating that no individual feature of the tetherin sequence is dispensable in the context of its lipid raft organising function.

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Section: Discussionmentioning

confidence: 99%

CD317/Tetherin is an organiser of membrane microdomains

Billcliff

Rollason

Prior

et al. 2013

Journal of Cell Science

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“…*P < 0.05, **P < 0.01, and ***P < 0.001. such as CCND1 63,64 and C/EBPb, 65 we also identified several novel PRL-induced genes, such as dexamethasoneinduced Ras-related protein 1 (RASD1), MYADM, and ZYX. These novel PRL-induced target genes are significant for the following reasons: i) RASD1 functions as a tumor suppressor gene by inhibiting cell growth, 66 ii) MYADM is important for the organization of lamellipodium extension and cell motility, 67 and iii) reports suggest that ZYX is a critical regulator of DNA damageeinduced cell death induction. 68 The role of such genes in normal and malignant processes within the mammary gland requires further characterization, but it will ultimately contribute to the overall knowledge of the complex PRL/PRLr signaling network.…”

Section: Discussionmentioning

confidence: 99%

The Prolactin Receptor Transactivation Domain Is Associated with Steroid Hormone Receptor Expression and Malignant Progression of Breast Cancer

Fiorillo

Medler

Feeney

et al. 2013

The American Journal of Pathology

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“…The human genome includes 28 MARVEL-containing open reading frames (Sánchez-Pulido et al, 2002;Aranda et al, 2011). Myelin and lymphocyteassociated protein (MAL) (Magal et al, 2009) is the first and best characterized MARVEL-domain protein (Millán et al, 1997;Puertollano et al, 1999;Sánchez-Pulido et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

The MARVEL transmembrane motif of occludin mediates oligomerization and targeting to the basolateral surface in epithelia

Yaffe

Shepshelovitch

Nevo-Yassaf

et al. 2012

Journal of Cell Science

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SummaryOccludin (Ocln), a MARVEL-motif-containing protein, is found in all tight junctions. MARVEL motifs are comprised of four transmembrane helices associated with the localization to or formation of diverse membrane subdomains by interacting with the proximal lipid environment. The functions of the Ocln MARVEL motif are unknown. Bioinformatics sequence-and structure-based analyses demonstrated that the MARVEL domain of Ocln family proteins has distinct evolutionarily conserved sequence features that are consistent with its basolateral membrane localization. Live-cell microscopy, fluorescence resonance energy transfer (FRET) and bimolecular fluorescence complementation (BiFC) were used to analyze the intracellular distribution and self-association of fluorescentprotein-tagged full-length human Ocln or the Ocln MARVEL motif excluding the cytosolic C-and N-termini (amino acids 60-269, FP-MARVEL-Ocln). FP-MARVEL-Ocln efficiently arrived at the plasma membrane (PM) and was sorted to the basolateral PM in filtergrown polarized MDCK cells. A series of conserved aromatic amino acids within the MARVEL domain were found to be associated with Ocln dimerization using BiFC. FP-MARVEL-Ocln inhibited membrane pore growth during Triton-X-100-induced solubilization and was shown to increase the membrane-ordered state using Laurdan, a lipid dye. These data demonstrate that the Ocln MARVEL domain mediates self-association and correct sorting to the basolateral membrane.

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

Cited by 46 publications

References 48 publications

CD317/Tetherin is an organiser of membrane microdomains

CD317/Tetherin is an organiser of membrane microdomains

The Prolactin Receptor Transactivation Domain Is Associated with Steroid Hormone Receptor Expression and Malignant Progression of Breast Cancer

The MARVEL transmembrane motif of occludin mediates oligomerization and targeting to the basolateral surface in epithelia

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