scholarly journals Alternative Splicing, Expression, and Genomic Structure of the 3′ Region of the Gene Encoding the Sarcolemmal-associated Proteins (SLAPs) Defines a Novel Class of Coiled-coil Tail-anchored Membrane Proteins

2000 ◽  
Vol 275 (49) ◽  
pp. 38474-38481 ◽  
Author(s):  
Paul A. Wielowieyski ◽  
Serdal Sevinc ◽  
Rosa Guzzo ◽  
Maysoon Salih ◽  
Jeffrey T. Wigle ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Membrane Proteins ◽  
Genomic Structure ◽  
Coiled Coil ◽  
Gene Encoding ◽  
Associated Proteins

TMCC3 localizes at the three-way junctions for the proper tubular network of the endoplasmic reticulum

2019 ◽  
Vol 476 (21) ◽  
pp. 3241-3260
Author(s):  
Sindhu Wisesa ◽  
Yasunori Yamamoto ◽  
Toshiaki Sakisaka
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Mammalian Cells ◽  
Coiled Coil ◽  
Transmembrane Domains ◽  
Domain Family ◽  
Coiled Coil Domain ◽  
U2os Cells ◽  
Er Membrane

The tubular network of the endoplasmic reticulum (ER) is formed by connecting ER tubules through three-way junctions. Two classes of the conserved ER membrane proteins, atlastins and lunapark, have been shown to reside at the three-way junctions so far and be involved in the generation and stabilization of the three-way junctions. In this study, we report TMCC3 (transmembrane and coiled-coil domain family 3), a member of the TEX28 family, as another ER membrane protein that resides at the three-way junctions in mammalian cells. When the TEX28 family members were transfected into U2OS cells, TMCC3 specifically localized at the three-way junctions in the peripheral ER. TMCC3 bound to atlastins through the C-terminal transmembrane domains. A TMCC3 mutant lacking the N-terminal coiled-coil domain abolished localization to the three-way junctions, suggesting that TMCC3 localized independently of binding to atlastins. TMCC3 knockdown caused a decrease in the number of three-way junctions and expansion of ER sheets, leading to a reduction of the tubular ER network in U2OS cells. The TMCC3 knockdown phenotype was partially rescued by the overexpression of atlastin-2, suggesting that TMCC3 knockdown would decrease the activity of atlastins. These results indicate that TMCC3 localizes at the three-way junctions for the proper tubular ER network.

Genomic structure, chromosome location, and alternative splicing of the humanNKG2A gene

1996 ◽  
Vol 44 (4) ◽  
pp. 286-291 ◽  
Author(s):  
Béatrice Plougastel ◽  
Tania Jones ◽  
John Trowsdale
Keyword(s):  
Alternative Splicing ◽  
Genomic Structure ◽  
Chromosome Location

scholarly journals Structural membrane proteins and loosely associated proteins of the sarcoplasmic reticulum

1974 ◽  
Vol 139 (3) ◽  
pp. 509-513 ◽  
Author(s):  
A. Margreth ◽  
U. Carraro ◽  
G. Salviati
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Membrane Proteins ◽  
Osmotic Shock ◽  
Protein Composition ◽  
Polyacrylamide Gels ◽  
Associated Proteins

The protein composition of sarcoplasmic-reticulum vesicles, either unpurified or after fractionation on sucrose gradients, and with or without previous osmotic shock and sonication, was investigated by electrophoresis in acid polyacrylamide gels. The pattern of release of loosely bound proteins is discussed with respect to their localization in the interior of the vesicles.

scholarly journals Lava Lamp, a Novel Peripheral Golgi Protein, Is Required for Drosophila melanogaster Cellularization

2000 ◽  
Vol 151 (4) ◽  
pp. 905-918 ◽  
Author(s):  
John C. Sisson ◽  
Christine Field ◽  
Richard Ventura ◽  
Anne Royou ◽  
William Sullivan
Keyword(s):  
Membrane Trafficking ◽  
Biochemical Analysis ◽  
Potent Inhibitor ◽  
Animal Cell ◽  
Coiled Coil ◽  
Brefeldin A ◽  
Microtubule Associated Proteins ◽  
Golgi Bodies ◽  
Associated Proteins ◽  
Golgi Protein

Drosophila cellularization and animal cell cytokinesis rely on the coordinated functions of the microfilament and microtubule cytoskeletal systems. To identify new proteins involved in cellularization and cytokinesis, we have conducted a biochemical screen for microfilament/microtubule-associated proteins (MMAPs). 17 MMAPs were identified; seven have been previously implicated in cellularization and/or cytokinesis, including KLP3A, Anillin, Septins, and Dynamin. We now show that a novel MMAP, Lava Lamp (Lva), is also required for cellularization. Lva is a coiled-coil protein and, unlike other proteins previously implicated in cellularization or cytokinesis, it is Golgi associated. Our functional analysis shows that cellularization is dramatically inhibited upon injecting anti–Lva antibodies (IgG and Fab) into embryos. In addition, we show that brefeldin A, a potent inhibitor of membrane trafficking, also inhibits cellularization. Biochemical analysis demonstrates that Lva physically interacts with the MMAPs Spectrin and CLIP190. We suggest that Lva and Spectrin may form a Golgi-based scaffold that mediates the interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization. Our results are consistent with the idea that animal cell cytokinesis depends on both actomyosin-based contraction and Golgi-derived membrane secretion.

scholarly journals Tailoring of Membrane Proteins by Alternative Splicing of Pre-mRNA

Biochemistry ◽  
2012 ◽  
Vol 51 (28) ◽  
pp. 5541-5556 ◽  
Author(s):  
Kathleen F. Mittendorf ◽  
Catherine L. Deatherage ◽  
Melanie D. Ohi ◽  
Charles R. Sanders
Keyword(s):  
Alternative Splicing ◽  
Membrane Proteins

The gene encoding a major component of the lateral elements of synaptonemal complexes of the rat is related to X-linked lymphocyte-regulated genes

1994 ◽  
Vol 14 (2) ◽  
pp. 1137-1146
Author(s):  
J H Lammers ◽  
H H Offenberg ◽  
M van Aalderen ◽  
A C Vink ◽  
A J Dietrich ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Similarity ◽  
Sodium Dodecyl ◽  
Coiled Coil ◽  
Amino Acid Identity ◽  
Male Rat ◽  
Amino Acid Sequence Similarity ◽  
Gene Encoding ◽  
Synaptonemal Complexes ◽  
Complex Protein

The lateral elements of synaptonemal complexes (SCs) of the rat contain major components with relative electrophoretic mobilities (M(r)S) of 30,000 and 33,000. After one-dimensional separation of SC proteins on polyacrylamide-sodium dodecyl sulfate gels, these components show up as two broad bands. These bands contain closely related proteins, as judged from their peptide maps and immunological reactivity. Using affinity-purified polyclonal anti-30,000- and anti-33,000-M(r) component antibodies, we isolated a cDNA encoding at least one of the 30,000- or 33,000-M(r) SC components. The protein predicted from the nucleotide sequence of the cDNA, called SCP3 (for synaptonemal complex protein 3), has a molecular mass of 29.7 kDa and a pI value of 9.4. It has a potential nucleotide binding site and contains stretches that are predicted to be capable of forming coiled-coil structures. In the male rat, the gene encoding SCP3 is transcribed exclusively in the testis. SCP3 has significant amino acid similarity to the pM1 protein, which is one of the predicted products of an X-linked lymphocyte-regulated gene family of the mouse: there are 63% amino acid sequence similarity and 35% amino acid identity between the SCP3 and pM1 proteins. However, SCP3 differs from pM1 in several respects, and whether the proteins fulfill related functions is still an open question.

scholarly journals The Fusion of Lipid and DNA Nanotechnology

Genes ◽  
2019 ◽  
Vol 10 (12) ◽  
pp. 1001 ◽  
Author(s):  
Es Darley ◽  
Jasleen Kaur Daljit Singh ◽  
Natalie A. Surace ◽  
Shelley F. J. Wickham ◽  
Matthew A. B. Baker
Keyword(s):  
Membrane Proteins ◽  
Lipid Membranes ◽  
Dna Nanotechnology ◽  
Bilayer Membrane ◽  
Diverse Range ◽  
Impermeable Barrier ◽  
Self Assembling ◽  
Associated Proteins ◽  
Fundamental Biological Process

Lipid membranes form the boundary of many biological compartments, including organelles and cells. Consisting of two leaflets of amphipathic molecules, the bilayer membrane forms an impermeable barrier to ions and small molecules. Controlled transport of molecules across lipid membranes is a fundamental biological process that is facilitated by a diverse range of membrane proteins, including ion-channels and pores. However, biological membranes and their associated proteins are challenging to experimentally characterize. These challenges have motivated recent advances in nanotechnology towards building and manipulating synthetic lipid systems. Liposomes—aqueous droplets enclosed by a bilayer membrane—can be synthesised in vitro and used as a synthetic model for the cell membrane. In DNA nanotechnology, DNA is used as programmable building material for self-assembling biocompatible nanostructures. DNA nanostructures can be functionalised with hydrophobic chemical modifications, which bind to or bridge lipid membranes. Here, we review approaches that combine techniques from lipid and DNA nanotechnology to engineer the topography, permeability, and surface interactions of membranes, and to direct the fusion and formation of liposomes. These approaches have been used to study the properties of membrane proteins, to build biosensors, and as a pathway towards assembling synthetic multicellular systems.

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