Evolutionary Analysis and Expression of Teleost Thy-1

Reuter, Alexander; Málaga-Trillo, Edward; Binkle, Ulrike; Rivera-Milla, Eric; Beltre, Rosanna; Zhou, Yi; Bastmeyer, Martin; Stuermer, Claudia A. O.

doi:10.1089/zeb.2004.1.191

Cited by 4 publications

(2 citation statements)

References 36 publications

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“…In mammals, IgSF members have evolved by mutation and selection into hundreds of proteins that are involved in diverse physiological functions, such as growth and development, signal transduction, cell adhesion, development of nervous system and protein–carbohydrate interactions (Amit et al ., 1986; Teichmann & Chothia, 2000; Reuter et al ., 2004; Fujimura et al ., 2006; Chen et al ., 2007; Cui et al ., 2007; Orazizadeh & Salter, 2007; Ossiboff & Parker, 2007; Camacho‐Leal & Stanners, 2008). IgSF proteins account for more than 2% of the total human genes, forming the largest gene family in the human genome (Srinivasan & Roeske, 2005).…”

Section: Introductionmentioning

confidence: 99%

Immunoglobulin superfamily is conserved but evolved rapidly and is active in the silkworm, Bombyx mori

Huang

Cheng

et al. 2009

Insect Molecular Biology

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Immunoglobulin superfamily (IgSF) proteins are known for their abilities to specifically recognize and adhere to cells. In this paper, we predicted the presence of 133 IgSF proteins in the silkworm (Bombyx mori) genome. Comparison with similar proteins in other model organisms (Caenorhabditis elegans, Drosophila melanogaster, Anopheles gambiae, Apis mellifera and Homo sapiens) indicated that IgSF proteins are conserved but have rapidly evolved from worms to human beings. However, these proteins are well conserved amongst insects. Silkworm microarray-based expression data showed tissue expression of 57 IgSF genes and microbe-induced differential expression of 37 genes. Based on the expression data, we can conclude that the silkworm IgSF is active.

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Section: Introductionmentioning

confidence: 99%

Immunoglobulin superfamily is conserved but evolved rapidly and is active in the silkworm, Bombyx mori

Huang

Cheng

et al. 2009

Insect Molecular Biology

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“…Reggies were isolated by co-immunoprecipitation with the monoclonal antibody M802, which was later shown to recognize the fish homologue of Thy-1 [3,4,53]. Fish Thy-1 co-localizes with reggies [54]. The close association with Thy-1 is conserved in different mammalian cell types such as PC12 and lymphocytes [29].…”

Section: Cellular Function Of Reggie Proteinsmentioning

confidence: 99%

Scaffolding microdomains and beyond: the function of reggie/flotillin proteins

Langhorst

Reuter

Stuermer

2005

Cell. Mol. Life Sci.

293

280

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Abstract. Reggie/flotillin proteins are considered to be components of lipid rafts and are commonly used as marker proteins for lipid microdomains. Yet almost a decade after their discovery, the function of reggies/ flotillins is still enigmatic. In this review we summarize the present state of knowledge on reggie/flotillin structure, localization and function, and discuss the role of the proteins in development and disease. Based on insights into reggie/flotillin function and by comparison with related proteins of the so-called SPFH (Stomatin/Prohibitin/ CMLS, Cell. Mol. Life Sci. 62 (2005) 2228-2240 1420-682X/05/202228-13 DOI 10.1007/s00018-005-5166-4 © Birkhäuser Verlag, Basel, 2005 Flotillin/HflK/C) protein family, including stomatin, podocin and prohibitin, we propose the existence of specific types of protein-defined microdomains which are sculpt by the clustering of individual SPFH proteins. As 'specialized rafts' similar to caveolae, these membrane domains provide platforms for the recruitment of multiprotein complexes. Since, under certain circumstances, reggie-2/flotillin-1 translocates to the nucleus, reggie/ flotillin microdomains are not only stable scaffolds but also dynamic units with their own regulatory functions.Key words. Lipid raft microdomains; signaling scaffolds; actin cytoskeleton; SPFH domain; stomatin; podocin; prohibitin; caveolae. Discovery of reggie/flotillins'Third time is a charm' the saying goes, and accordingly, reggie/flotillin proteins were independently 'discovered' three times. Madeleine Duvic and co-workers were the very first to discover part of one of the proteins during a screen for the antigen of the monoclonal antibody ECS-1 in 1994. They identified a complementary DNA (cDNA) coding for a N-terminally truncated version of reggie-1/flotillin-2 of 42 kDa (see below), which they called epidermal surface antigen (ESA) [1]. This name was later abandoned, as it was shown that this protein is not the true antigen recognized by ECS-1 [2]. In a screen for proteins upregulated in retinal ganglion cells during axon regeneration after optic nerve lesion in goldfish, we identified in 1997 two proteins of 47 kDa which we called reggie-1 and -2 [3,4]. In the same year Michael Lisanti's group identified two proteins associated with the 'floating' lipid raft fraction from mouse lung tissue which they called flotillin-1 (= reggie-2) and flotillin-2 (= reggie-1) [5]. Although flotillins became the more commonly used name for the proteins, we will stick with reggie-1 and -2, since we believe that our names and numbers are more appropriate in light of the physiological relevance of the two proteins. Structure of reggiesReggie proteins are highly conserved, with about 64% homology between fly and man [6,7]. Reggie-like proteins even exist in some bacteria, plants and fungi [8,9].

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Microdomain-forming proteins and the role of the reggies/flotillins during axon regeneration in zebrafish

Stuermer¹

2011

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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The two proteins reggie-1 and reggie-2 (flotillins) were identified in axon-regenerating neurons in the central nervous system and shown to be essential for neurite growth and regeneration in fish and mammals. Reggies/flotillins are microdomain scaffolding proteins sharing biochemical properties with lipid raft molecules, form clusters at the cytoplasmic face of the plasma membrane and interact with signaling molecules in a cell type specific manner. In this review, reggie microdomains, lipid rafts, related scaffolding proteins and caveolin-which, however, are responsible for their own microdomains and functions-are introduced. Moreover, the function of the reggies in axon growth is demonstrated: neurons fail to extend axons after reggie knockdown. Furthermore, our current concept of the molecular mechanism underlying reggie function is presented: the association of glycosyl-phophatidyl inositol (GPJ)-anchored surface proteins with reggie microdomains elicits signals which activate src tyrosine and mitogen-activated protein kinases, as well as small guanosine 5'-triphosphate-hydrolyzing enzymes. This leads to the mobilization of intracellular vesicles and to the recruitment of bulk membrane and specific cargo proteins, such as cadherin, to specific sites of the plasma membrane such as the growth cone of elongating axons. Thus, reggies regulate the targeted delivery of cargo-a process which is required for process extension and growth. This article is part of a Special Issue entitled Zebrafish Models of Neurological Diseases.

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Evolutionary Analysis and Expression of Teleost Thy-1

Cited by 4 publications

References 36 publications

Immunoglobulin superfamily is conserved but evolved rapidly and is active in the silkworm, Bombyx mori

Immunoglobulin superfamily is conserved but evolved rapidly and is active in the silkworm, Bombyx mori

Scaffolding microdomains and beyond: the function of reggie/flotillin proteins

Microdomain-forming proteins and the role of the reggies/flotillins during axon regeneration in zebrafish

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