scholarly journals The defective kernel 1 (dek1) gene required for aleurone cell development in the endosperm of maize grains encodes a membrane protein of the calpain gene superfamily

2002 ◽  
Vol 99 (8) ◽  
pp. 5460-5465 ◽  
Author(s):  
S. E. Lid ◽  
D. Gruis ◽  
R. Jung ◽  
J. A. Lorentzen ◽  
E. Ananiev ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cell Development ◽  
Aleurone Cell ◽  
Calpain Gene

scholarly journals Epstein-Barr virus latent membrane protein 2A exploits Notch1 to alter B-cell identity in vivo

Blood ◽  
2009 ◽  
Vol 113 (1) ◽  
pp. 108-116 ◽  
Author(s):  
Leah J. Anderson ◽  
Richard Longnecker
Keyword(s):  
Membrane Protein ◽  
B Cell ◽  
Epstein Barr Virus ◽  
Cell Development ◽  
B Cell Development ◽  
Latent Membrane Protein ◽  
Cell Identity ◽  
Barr Virus ◽  
Epstein Barr

Abstract Expression of latent membrane protein 2 (LMP2A) during B-cell development leads to global alterations in gene transcription similar to those seen in Hodgkin Reed-Sternberg cells of Hodgkin lymphoma (HL). Along with the consistent detection of LMP2A in Epstein-Barr virus–associated HL, this implicates a role for LMP2A in the pathogenesis of HL. We have shown that LMP2A constitutively activates the Notch1 pathway to autoregulate the LMP2A promoter. To determine whether constitutive activation of the Notch pathway is important for LMP2A-mediated alterations in B-cell development in vivo, TgE-LMP2A–transgenic mice were intercrossed with mice expressing loxP-flanked Notch1 genes and Cre recombinase. B cells from TgE Notch1lox/lox-CD19+/Cre mice have an increase in immunoglobulin M and CD43 and a decrease in CD5 expression in the bone marrow compared with TgE Notch1lox/lox mice, indicating the LMP2A signal for developmental aberrations is impaired in the absence of Notch1. Real-time reverse-transcribed polymerase chain reaction analysis reveals that LMP2A requires the Notch1 pathway to alter levels of B cell–specific transcription factors, E2A and EBF. Interestingly, Notch1 appears to be important for LMP2A-mediated survival in low interleukin-7. We propose that LMP2A and the Notch1 pathway may cooperate to induce the alterations in B-cell identity seen in Hodgkin Reed-Sternberg cells.

scholarly journals Latent Membrane Protein 2A, a Viral B Cell Receptor Homologue, Induces CD5+B-1 Cell Development

2004 ◽  
Vol 172 (9) ◽  
pp. 5329-5337 ◽  
Author(s):  
Akiko Ikeda ◽  
Mark Merchant ◽  
Lori Lev ◽  
Richard Longnecker ◽  
Masato Ikeda
Keyword(s):  
Membrane Protein ◽  
B Cell ◽  
Cell Receptor ◽  
Cell Development ◽  
Latent Membrane Protein ◽  
B Cell Receptor ◽  
Latent Membrane Protein 2A

shrunken4 is a mutant allele of ZmYSL2 that affects aleurone development and starch synthesis in maize

Genetics ◽  
2021 ◽  
Author(s):  
Yonghui He ◽  
Qing Yang ◽  
Jun Yang ◽  
Yong-Fei Wang ◽  
Xiaoliang Sun ◽  
...  
Keyword(s):  
Seed Development ◽  
Starch Synthesis ◽  
Cell Activity ◽  
Cell Development ◽  
Endosperm Development ◽  
Xenopus Laevis Oocytes ◽  
Aleurone Layer ◽  
Maize Seed ◽  
Starchy Endosperm ◽  
Aleurone Cell

Abstract Minerals are stored in the aleurone layer and embryo during maize seed development, but how they affect endosperm development and activity is unclear. Here, we cloned the gene underlying the classic maize kernel mutant shrunken4 (sh4) and found that it encodes the YELLOW STRIPE-LIKE oligopeptide metal transporter ZmYSL2. sh4 kernels had a shrunken phenotype with developmental defects in the aleurone layer and starchy endosperm cells. ZmYSL2 showed iron and zinc transporter activity in Xenopus laevis oocytes. Analysis using a specific antibody indicated that ZmYSL2 predominately accumulated in the aleurone and sub-aleurone layers in endosperm and the scutellum in embryos. Specific iron deposition was observed in the aleurone layer in wild-type kernels. In sh4, however, the outermost monolayer of endosperm cells failed to accumulate iron and lost aleurone cell characteristics, indicating that proper functioning of ZmYSL2 and iron accumulation are essential for aleurone cell development. Transcriptome analysis of sh4 endosperm revealed that loss of ZmYSL2 function affects the expression of genes involved in starch synthesis and degradation processes, which is consistent with the delayed development and premature degradation of starch grains in sh4 kernels. Therefore, ZmYSL2 is critical for aleurone cell development and starchy endosperm cell activity during maize seed development.

Barley aleurone cell development: molecular cloning of aleurone-specific cDNAs from immature grains

1989 ◽  
Vol 12 (3) ◽  
pp. 285-293 ◽  
Author(s):  
Kjetill Jakobsen ◽  
Sonja Sletner Klemsdal ◽  
Reidunn B. Aalen ◽  
Marie Bosnes ◽  
Danny Alexander ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Cell Development ◽  
Aleurone Cell ◽  
Barley Aleurone

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.

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