Myelin and lymphocyte protein (MAL/MVP17/VIP17) and plasmolipin are members of an extended gene family

Magyar, Josef P.; Ebensperger, Christoph; Schaeren‐Wiemers, Nicole; Suter, Ueli

doi:10.1016/s0378-1119(96)00861-x

Cited by 52 publications

(57 citation statements)

References 23 publications

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“…A possible sea squirt MAL protein was identified with frog MAL as query (scaffold 20, ci0100134996). A reciprocal BLASTP search with this model sequence identified a conserved MARVEL domain (characteristic of MAL) and matches to MAL family members including plasmolipin (Magyar et al, 1997) and chemokine-like factor super family (CLF)-8 proteins (Han et al, 2003). Models from other Ciona hits were found to be unrelated to MAL family proteins in the reciprocal BLASTP searches.…”

Section: Among Myelin-related Proteins Mal/plasmolipin and Pmp22 Bumentioning

confidence: 94%

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Myelin Tetraspan Family Proteins but No Non-Tetraspan Family Proteins Are Present in the Ascidian (Ciona intestinalis) Genome

Gould

Morrison²,

Gilland³

et al. 2005

The Biological Bulletin

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Abstract. Several of the proteins used to form and maintain myelin sheaths in the central nervous system (CNS) and the peripheral nervous system (PNS) are shared among different vertebrate classes. These proteins include one-toseveral alternatively spliced myelin basic protein (MBP) isoforms in all sheaths, proteolipid protein (PLP) and DM20 (except in amphibians) in tetrapod CNS sheaths, and one or two protein zero (P 0 ) isoforms in fish CNS and in all vertebrate PNS sheaths. Several other proteins, including 2Ј, 3Ј-cyclic nucleotide 3Ј-phosphodiesterase (CNP), myelin and lymphocyte protein (MAL), plasmolipin, and peripheral myelin protein 22 (PMP22; prominent in PNS myelin), are localized to myelin and myelin-associated membranes, though class distributions are less well studied. Databases with known and identified sequences of these proteins from cartilaginous and teleost fishes, amphibians, reptiles, birds, and mammals were prepared and used to search for potential homologs in the basal vertebrate, Ciona intestinalis. Homologs of lipophilin proteins, MAL/plasmolipin, and PMP22 were identified in the Ciona genome. In contrast, no MBP, P 0 , or CNP homologs were found. These studies provide a framework for understanding how myelin proteins were recruited during evolution and how structural adaptations enabled them to play key roles in myelination.

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Section: Among Myelin-related Proteins Mal/plasmolipin and Pmp22 Bumentioning

confidence: 94%

“…2). Seven of eight additional amino acids for MAL/plasmolipin/BENE proteins (Magyar et al, 1997) are conserved in sea squirt PL-1 (Fig. 2).…”

Section: Among Myelin-related Proteins Mal/plasmolipin and Pmp22 Bumentioning

confidence: 99%

Myelin Tetraspan Family Proteins but No Non-Tetraspan Family Proteins Are Present in the Ascidian (Ciona intestinalis) Genome

Gould

Morrison²,

Gilland³

et al. 2005

The Biological Bulletin

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“…33 BENE belongs to the MAL family, which is widely expressed in various tissues, suggesting a common role of these proteins in cell biology. 34 MCM4, a DNA-replication-initiation factor, is an essential component of a protein complex that prevents DNA from being replicated more than once per cell cycle. 35 To our knowledge, neither BENE nor MCM4 genes have been previously studied in cancer.…”

Section: Genes With Other Functionsmentioning

confidence: 99%

Expression profiling of gastric adenocarcinoma using cDNA array

et al. 2001

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To investigate the expression profile of gastric adenocarcinoma, cDNA array experiments were performed using Atlas Human Cancer 1.2 K Array (Clontech Laboratories, Palo Alto, CA) on nine xenografted and two primary gastric cancer samples. The expression of the tumor samples was compared to that of two normal gastric epithelial tissues. The expression pattern of the primary tumors was similar to that of xenografted tumors. The up-regulated genes had expression ratios ranging from 2.5 to 16, whereas the down-regulated genes had a range from ؊2.5 to ؊16. No variation in gene expression was detected in the analysis of the xenografted tumors versus the primary tumors, indicating that the xenografts represented the primary tumors well. Thirtyeight genes showed altered gene expression in 5 or more samples (>45%). Thirty-one genes were up-regulated and seven genes were down-regulated. The most abundantly upregulated genes (ratio >5) included genes such as S100A4, CDK4, MMP14 and beta catenin. The GIF was markedly downregulated (ratio < ؊10). To confirm our findings, six genes (three up-and three down-regulated) were selected for semiquantitative RT-PCR analysis. The RT-PCR results were consistent with the array findings. Our approach revealed that several genes are abnormally expressed in gastric cancer and found that genes known to interact in several common molecular pathway(s) were consistently altered. © 2001 Wiley-Liss, Inc. Key words: cDNA arrays; gene expression; xenografts; and gastric adenocarcinomasGastric carcinoma (GC) is one of the most common malignancies worldwide and is the second most common cause of cancerrelated death. 1 Overall relative 5-year survival rates are currently less than 20%. Cytogenetic studies of gastric adenocarcinomas are few in number and have failed to identify any consistent or noteworthy chromosomal abnormalities. 2 Comprehensive studies of DNA copy number changes using comparative genomic hybridization (CGH) have revealed alterations in several chromosomal regions. 3-5 Frequent high-level amplifications were noted at 17q and 20q, whereas DNA copy number losses were frequently seen in 4q, 5q, and 9p. However, there are few data on gene expression in gastric cancer. The recent development of cDNA array technology allows the study of gene expression level and gene activation in thousands of genes and sequences. 6,7 The data obtained from the array analysis are expected to uncover novel genes related to cancer development and its clinical behavior. However, tumor sample contamination with normal cells makes analysis of hundreds of genes more difficult and less sensitive. Xenografting of human tumors has been used to produce optimal samples that are enriched for neoplastic cells for subsequent molecular analyses.

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“…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). MAL is a small (17 kDa) membrane protein that is an obligatory component of cellular processes such as the apical sorting machinery, the immunological synapse in activated T cells (Martín-Belmonte et al, 1998;Antón et al, 2008) and myelin formation and maintenance (Magyar et al, 1997). The MARVEL domain of MAL is associated with the generation and stabilization of functional membrane domains via its propensity for homo-oligomerization and its ability to attract apical membrane lipids.…”

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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Myelin and lymphocyte protein (MAL/MVP17/VIP17) and plasmolipin are members of an extended gene family

Cited by 52 publications

References 23 publications

Myelin Tetraspan Family Proteins but No Non-Tetraspan Family Proteins Are Present in the Ascidian (Ciona intestinalis) Genome

Myelin Tetraspan Family Proteins but No Non-Tetraspan Family Proteins Are Present in the Ascidian (Ciona intestinalis) Genome

Expression profiling of gastric adenocarcinoma using cDNA array

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

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