Proteome Analysis of Lipid Rafts in Jurkat Cells Characterizes a Raft Subset That Is Involved in NF-κB Activation

Tu, Xiaolin; Huang, Aaron; Bae, David; Slaughter, Ndaisha; Whitelegge, Julian P.; Crother, Timothy R.; Bickel, Perry E.; Nel, André E.

doi:10.1021/pr0340779

Cited by 36 publications

(43 citation statements)

References 64 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Insoluble subfractions 1 to 6, and soluble fraction 6 are depicted and were exposed to film simultaneously as part of the same gel. Li et al, 2003;Mielenz et al, 2005;Nebl et al, 2002;Tu et al, 2004;Wollscheid et al, 2004). Some of these studies have identified erlin-1 and erlin-2 within lipid raft fractions of a number of cell types but very little if any information regarding their biochemical and molecular characterization is available Blonder et al, 2004b;Blonder et al, 2004c;Ledesma et al, 2003;Sprenger et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER

Browman

Resek

Zajchowski

et al. 2006

Journal of Cell Science

198

204

View full text Add to dashboard Cite

Our laboratory was interested in characterizing the molecular composition of non-caveolar lipid rafts. Thus, we generated monoclonal antibodies to lipid raft proteins of human myelomonocytic cells. Two of these proteins, KE04p and C8orf2, were found to be highly enriched in the detergent-insoluble, buoyant fraction of sucrose gradients in a cholesterol-dependent manner. They contain an evolutionarily conserved domain placing them in the prohibitin family of proteins. In contrast to other family members, these two proteins localized to the ER. Furthermore, the extreme N-termini of KE04p and C8orf2 were found to be sufficient for heterologous targeting of GFP to the ER in the absence of classical ER retrieval motifs. We also demonstrate that all prohibitin family members rely on sequences in their extreme N-termini for their distinctive subcellular distributions including the mitochondria, plasma membrane and Golgi vesicles. Owing to their subcellular localization and their presence in lipid rafts, we have named KE04p and C8orf2, ER lipid raft protein (erlin)-1 and erlin-2, respectively. Interestingly, the ER contains relatively low levels of cholesterol and sphingolipids compared with other organelles. Thus, our data support the existence of lipid-raft-like domains within the membranes of the ER.

show abstract

Section: Discussionmentioning

confidence: 99%

Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER

Browman

Resek

Zajchowski

et al. 2006

Journal of Cell Science

198

204

View full text Add to dashboard Cite

show abstract

“…Both reggies are expressed in B and T lymphocytes [17,29]. In T cells, reggie-1 and -2 are associated with the Src-kinases lck and fyn as shown by co-immunoprecipitation [29,31,42,62]. Reggie-2 binds fyn regardless of its activity, as it also binds to the kinase-dead mutant [41].…”

Section: Cellular Function Of Reggie Proteinsmentioning

confidence: 99%

“…Furthermore, reggies are associated with the adaptor protein LAT [42]. The association with LAT and lck apparently increases after CD3/CD28 co-stimulation of the cell; furthermore vimentin and IKKb associate with reggie complexes after activation of the cell [42,62]. Both in stable cell lines and in peripheral lymphocytes, reggie-1 and -2 exhibit a strikingly polarized localization in resting cells, accumulating in one aspect of the cell forming a 'preformed cap' [31,63].…”

Section: Cellular Function Of Reggie Proteinsmentioning

confidence: 99%

See 1 more Smart Citation

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

Langhorst

Reuter

Stuermer

2005

Cell. Mol. Life Sci.

290

280

View full text Add to dashboard Cite

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].

show abstract

“…[158]. 2-DE allowed Tu et al [161] to provide evidence that a subset of lipid rafts is involved in NF-kB activation, which is an important finding in cellular signaling pathway.…”

Section: Leukocytesmentioning

confidence: 99%

Recent advances in blood‐related proteomics

et al. 2005

View full text Add to dashboard Cite

Service régional vaudois de transfusion sanguine, Lausanne, SwitzerlandBlood is divided in two compartments, namely, plasma and cells. The latter contain red blood cells, leukocytes, and platelets. From a descriptive medical discipline, hematology has evolved towards a pioneering discipline where molecular biology has permitted the development of prognostic and diagnostic indicators for disease. The recent advance in MS and protein separation now allows similar progress in the analysis of proteins. Proteomics offers great promise for the study of proteins in plasma/serum, indeed a number of proteomics databases for plasma/ serum have been established. This is a very complex body fluid containing lipids, carbohydrates, amino acids, vitamins, nucleic acids, hormones, and proteins. About 1500 different proteins have recently been identified, and a number of potential new markers of diseases have been characterized. Here, examples of the enormous promise of plasma/serum proteomic analysis for diagnostic/prognostic markers and information on disease mechanism are given. Within the blood are also a large number of different blood cell types that potentially hold similar information. Proteomics of red blood cells, until now, has not improved our knowledge of these cells, in contrast to the major progresses achieved while studying platelets and leukocytes. In the future, proteomics will change several aspects of hematology.

show abstract

Proteome Analysis of Lipid Rafts in Jurkat Cells Characterizes a Raft Subset That Is Involved in NF-κB Activation

Cited by 36 publications

References 64 publications

Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER

Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER

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

Recent advances in blood‐related proteomics

Contact Info

Product

Resources

About