scholarly journals Evolutionary and Functional Analysis of a Chara Plasma Membrane H+-ATPase

2020 ◽  
Vol 10 ◽  
Author(s):  
Suyun Zhang ◽  
Myckel Habets ◽  
Holger Breuninger ◽  
Liam Dolan ◽  
Remko Offringa ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Plasma Membrane

The Candida albicans plasma membrane protein Rch1p, a member of the vertebrate SLC10 carrier family, is a novel regulator of cytosolic Ca2+ homoeostasis

2012 ◽  
Vol 444 (3) ◽  
pp. 497-502 ◽  
Author(s):  
Linghuo Jiang ◽  
Joerg Alber ◽  
Jihong Wang ◽  
Wei Du ◽  
Xuexue Yang ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Candida Albicans ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Solute Carrier Family ◽  
Plasma Membrane Protein ◽  
Cellular Functions ◽  
Downstream Target ◽  
Solute Carrier ◽  
High Concentrations

Candida albicans RCH1 (regulator of Ca2+ homoeostasis 1) encodes a protein of ten TM (transmembrane) domains, homologous with human SLC10A7 (solute carrier family 10 member 7), and Rch1p localizes in the plasma membrane. Deletion of RCH1 confers hypersensitivity to high concentrations of extracellular Ca2+ and tolerance to azoles and Li+, which phenocopies the deletion of CaPMC1 (C. albicans PMC1) encoding the vacuolar Ca2+ pump. Additive to CaPMC1 mutation, lack of RCH1 alone shows an increase in Ca2+ sensitivity, Ca2+ uptake and cytosolic Ca2+ level. The Ca2+ hypersensitivity is abolished by cyclosporin A and magnesium. In addition, deletion of RCH1 elevates the expression of CaUTR2 (C. albicans UTR2), a downstream target of the Ca2+/calcineurin signalling. Mutational and functional analysis indicates that the Rch1p TM8 domain, but not the TM9 and TM10 domains, are required for its protein stability, cellular functions and subcellular localization. Therefore Rch1p is a novel regulator of cytosolic Ca2+ homoeostasis, which expands the functional spectrum of the vertebrate SLC10 family.

scholarly journals A Comparative Functional Analysis of Plasma Membrane Ca2+Pump Isoforms in Intact Cells

2003 ◽  
Vol 278 (27) ◽  
pp. 24500-24508 ◽  
Author(s):  
Marisa Brini ◽  
Luisa Coletto ◽  
Nicola Pierobon ◽  
Natasha Kraev ◽  
Danilo Guerini ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Plasma Membrane ◽  
Intact Cells

scholarly journals Functional analysis of chimerical plasma membrane H+-ATPases fromSaccharomyces cerevisiaeandSchizosaccharomyces pombe

1997 ◽  
Vol 25 (02) ◽  
pp. 261-273 ◽  
Author(s):  
Alban de Kerchove d’Exaerde ◽  
Pierre Morsomme ◽  
Denise Sempoux-Thinès ◽  
Philip Supply ◽  
André Goffeau ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Plasma Membrane

scholarly journals Expression and functional analysis of the rice plasma-membrane intrinsic protein gene family

Cell Research ◽  
2006 ◽  
Vol 16 (3) ◽  
pp. 277-286 ◽  
Author(s):  
Lei Guo ◽  
Zi Yi Wang ◽  
Hong Lin ◽  
Wei Er Cui ◽  
Jun Chen ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Plasma Membrane ◽  
Gene Family ◽  
Protein Gene ◽  
Plasma Membrane Intrinsic Protein ◽  
Intrinsic Protein

scholarly journals The ternary complex CEP90, FOPNL and OFD1 specifies the future location of centriolar distal appendages, and promotes their assembly

2021 ◽  
Author(s):  
Pierrick Le Borgne ◽  
Marine Hélène Laporte ◽  
Logan Greibill ◽  
Michel Lemullois ◽  
Mebarek Temagoult ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Plasma Membrane ◽  
Transition Zone ◽  
Basal Body ◽  
Mammalian Cells ◽  
Ternary Complex ◽  
Basal Bodies ◽  
Sequence Of Events ◽  
The Future ◽  
High Conservation

Cilia assembly starts with centriole to basal body maturation, migration to the cell surface and docking to the plasma membrane. The basal body docking process involves the interaction of both the distal end of the basal body and the transition fibers (or mature distal appendages), with the plasma membrane. During this process, the transition zone assembles and forms the structural junction between the basal body and the nascent cilium. Mutations in numerous genes involved in basal body docking and transition zone assembly are associated with the most severe ciliopathies, highlighting the importance of these events in cilium biogenesis. The conservation of this sequence of events across phyla is paralleled by a high conservation of the proteins involved. We identified CEP90 by BioID using FOPNL as a bait. Ultrastructure expansion microscopy showed that CEP90, FOPNL and OFD1 localized at the distal end of both centrioles/basal bodies in Paramecium and mammalian cells. These proteins are recruited early after duplication on the procentriole. Finally, functional analysis performed both in Paramecium and mammalian cells demonstrate the requirement of this complex for distal appendage assembly and basal body docking. Altogether, we propose that this ternary complex is required to determine the future position of distal appendages

Isolation, expression, and functional analysis of developmentally regulated plasma membrane polypeptide 1 (DREPP1) in Sporobolus virginicus grown under alkali salt stress

PROTOPLASMA ◽  
2018 ◽  
Vol 255 (5) ◽  
pp. 1423-1432
Author(s):  
Cattarin Theerawitaya ◽  
Nana Yamada-Kato ◽  
Harminder Pal Singh ◽  
Suriyan Cha-um ◽  
Teruhiro Takabe
Keyword(s):  
Functional Analysis ◽  
Plasma Membrane ◽  
Salt Stress ◽  
Developmentally Regulated ◽  
Alkali Salt ◽  
Sporobolus Virginicus

Autosomal Recessive Hereditary Thrombocytosis: Functional Analysis of a Novel C-Mpl Mutation Resulting in An Unsual Mode of Constitutive Receptor Activation

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 890-890
Author(s):  
Clemens Stockklausner ◽  
Niels Gehring ◽  
Nicole Echner ◽  
Naima Ali Al Mulla ◽  
Andreas E. Kulozik
Keyword(s):  
Functional Analysis ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Negative Feedback ◽  
Plasma Levels ◽  
Feedback Loop ◽  
Negative Feedback Loop ◽  
Normal Range ◽  
Gain Of Function ◽  
Downstream Signaling

Abstract Thrombopoiesis is tightly regulated by the interaction between thrombopoietin (TPO) and its receptor c-Mpl. Ligand binding results in dimerization of the receptor, internalization of the complex, and activation of downstream signaling. This activation pathway also leads to the clearance of TPO from the plasma thus establishing a negative feedback loop. Gain of function mutations of TPO and c-Mpl are exceedingly rare but provide interesting models for the biological understanding of the molecular interactions that are required for a functional TPO pathway. Here, we describe a consanguineous Qatari family with hereditary thrombocytosis. Genotype analysis revealed a novel c-Mpl P106L mutation that was found homozygously in 3 affected patients with platelet counts between 700–800/nl. The TPO gene sequence was normal. Notably, platelet counts in heterozygous relatives were within the normal range. Surprisingly, TPO plasma levels were elevated to 10 to 15-fold in homozygotes but within the normal range in heterozygotes. A simple gain of function mechanism of the c-Mpl mutation could thus be excluded. Therefore, we next functionally analyzed and compared the normal and the P106L mutated c-Mpl receptor. An analysis of HeLa and BaF3 cells that were transiently or stably, respectively, transfected with c-Mpl expression vectors showed that the P106L mutation leads to abnormal subcellular receptor distribution. Whereas normal c-Mpl was detected in the Golgi-apparatus and in the plasma membrane, c-Mpl P106L was predominantly found within the ER. Furthermore, we showed that c-Mpl P106L cannot be processed to the normal, tunicamycin sensitive, strongly glycosylated form. Functional analysis of the TPO/c-Mpl signaling pathway in stably transfected BaF3 cells demonstrated an elevated phosphorylation of Stat5 with P106L when compared to normal c-Mpl. Moreover, cells transfected with the mutant but not with the normal receptor gene were proliferating independently of extracellular growth factors such as IL3. These data indicate that c-Mpl P106L activates downstream signaling and thus stimulates cell division and platelet production in a ligand-independent fashion. The recessive mode of inheritance suggests that the presence of normal receptor molecules prevents this abnormal function and promotes the maintenance of the negative feedback loop regulating TPO plasma levels by an unknown mechanism. The raised TPO plasma levels in homozygotes and the lack of detectable mutated c-Mpl in the plasma membrane indicate that the mutated receptor does not bind and internalize its normal ligand. In conclusion, we hypothesize that the novel c-Mpl P106L receptor mutation results in spontaneous dimerization and ligand independent activation even before the receptor reaches the Golgi apparatus and is fully glycosylated and transported to the plasma membrane.

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