scholarly journals A PEX5 missense allele preferentially disrupts PTS1 cargo import into Arabidopsis peroxisomes

Plant Direct ◽  
2019 ◽  
Vol 3 (3) ◽  
pp. e00128 ◽  
Author(s):  
Khushali J. Patel ◽  
Yun-Ting Kao ◽  
Roxanna J. Llinas ◽  
Bonnie Bartel
Keyword(s):  
Missense Allele

A missense allele of PEX5 is responsible for the defective import of PTS2 cargo proteins into peroxisomes

2021 ◽  
Author(s):  
Muhammad Ali ◽  
Shahid Y. Khan ◽  
Tony A. Rodrigues ◽  
Tânia Francisco ◽  
Xiaodong Jiao ◽  
...  
Keyword(s):  
Cargo Proteins ◽  
Missense Allele

scholarly journals Cross-species functional diversity within the PIN auxin efflux protein family

2016 ◽  
Author(s):  
Devin Lee O’Connor ◽  
Samuel Elton ◽  
Fabrizio Ticchiarelli ◽  
Mon Mandy Hsia ◽  
John Vogel ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Functional Diversity ◽  
Tissue Level ◽  
Stem Growth ◽  
Flowering Plants ◽  
Flower Formation ◽  
Transport Activity ◽  
Functional Specificity ◽  
Missense Allele ◽  
Vein Patterning

AbstractIn Arabidopsis, development during flowering is coordinated by transport of the hormone auxin mediated by polar-localized PIN-FORMED1 (AtPIN1). However Arabidopsis has lost a PIN clade sister to AtPIN1, Sister-of-PIN1 (SoPIN1), which is conserved in flowering plants. We previously proposed that the AtPIN1 organ initiation and vein patterning functions are split between the SoPIN1 and PIN1 clades in grasses. Here we show that in the grass Brachypodium sopin1 mutants have organ initiation defects similar to Arabidopsis atpin1, while loss of PIN1 function in Brachypodium has little effect on organ initiation but alters stem growth. Heterologous expression of Brachypodium SoPIN1 and PIN1b in Arabidopsis provides further evidence of functional specificity. SoPIN1 but not PIN1b can mediate flower formation in null atpin1 mutants, although both can complement a missense allele. The behavior of SoPIN1 and PIN1b in Arabidopsis illustrates how membrane and tissue-level accumulation, transport activity, and interaction contribute to PIN functional specificity.

scholarly journals A novel coordinated function of Myosin II with GOLPH3 controls centralspindlin localization during cytokinesis in Drosophila

2020 ◽  
Vol 133 (21) ◽  
pp. jcs252965
Author(s):  
Stefano Sechi ◽  
Anna Frappaolo ◽  
Angela Karimpour-Ghahnavieh ◽  
Roberta Fraschini ◽  
Maria Grazia Giansanti
Keyword(s):  
Plasma Membrane ◽  
Heavy Chain ◽  
Light Chain ◽  
Animal Cell ◽  
Myosin Ii ◽  
Contractile Ring ◽  
Ring Assembly ◽  
Missense Allele ◽  
Phosphatidylinositol 4 ◽  
Muscle Myosin

ABSTRACTIn animal cell cytokinesis, interaction of non-muscle myosin II (NMII) with F-actin provides the dominant force for pinching the mother cell into two daughters. Here we demonstrate that celibe (cbe) is a missense allele of zipper, which encodes the Drosophila Myosin heavy chain. Mutation of cbe impairs binding of Zipper protein to the regulatory light chain Spaghetti squash (Sqh). In dividing spermatocytes from cbe males, Sqh fails to concentrate at the equatorial cortex, resulting in thin actomyosin rings that are unable to constrict. We show that cbe mutation impairs localization of the phosphatidylinositol 4-phosphate [PI(4)P]-binding protein Golgi phosphoprotein 3 (GOLPH3, also known as Sauron) and maintenance of centralspindlin at the cell equator of telophase cells. Our results further demonstrate that GOLPH3 protein associates with Sqh and directly binds the centralspindlin subunit Pavarotti. We propose that during cytokinesis, the reciprocal dependence between Myosin and PI(4)P–GOLPH3 regulates centralspindlin stabilization at the invaginating plasma membrane and contractile ring assembly.

scholarly journals A viable Arabidopsis pex13 missense allele confers severe peroxisomal defects and decreases PEX5 association with peroxisomes

2014 ◽  
Vol 86 (1-2) ◽  
pp. 201-214 ◽  
Author(s):  
Andrew W. Woodward ◽  
Wendell A. Fleming ◽  
Sarah E. Burkhart ◽  
Sarah E. Ratzel ◽  
Marta Bjornson ◽  
...  
Keyword(s):  
Missense Allele

scholarly journals Intragenic complementation of amino and carboxy terminal SMN missense mutations can rescue Smn null mice

2020 ◽  
Author(s):  
Vicki L McGovern ◽  
Kaitlyn M Kray ◽  
W David Arnold ◽  
Sandra I Duque ◽  
Chitra C Iyer ◽  
...  
Keyword(s):  
Functional Unit ◽  
Muscular Atrophy ◽  
Missense Mutations ◽  
Wild Type ◽  
Sm Proteins ◽  
Intragenic Complementation ◽  
Missense Allele ◽  
Smn Protein ◽  
Neuron Electrophysiology ◽  
Carboxy Terminal

Abstract Spinal muscular atrophy is caused by reduced levels of SMN resulting from the loss of SMN1 and reliance on SMN2 for the production of SMN. Loss of SMN entirely is embryonic lethal in mammals. There are several SMN missense mutations found in humans. These alleles do not show partial function in the absence of wild-type SMN and cannot rescue a null Smn allele in mice. However, these human SMN missense allele transgenes can rescue a null Smn allele when SMN2 is present. We find that the N- and C-terminal regions constitute two independent domains of SMN that can be separated genetically and undergo intragenic complementation. These SMN protein heteromers restore snRNP assembly of Sm proteins onto snRNA and completely rescue both survival of Smn null mice and motor neuron electrophysiology demonstrating that the essential functional unit of SMN is the oligomer.

scholarly journals Human HOIP and LUBAC deficiency underlies autoinflammation, immunodeficiency, amylopectinosis, and lymphangiectasia

2015 ◽  
Vol 212 (6) ◽  
pp. 939-951 ◽  
Author(s):  
Bertrand Boisson ◽  
Emmanuel Laplantine ◽  
Kerry Dobbs ◽  
Aurélie Cobat ◽  
Nadine Tarantino ◽  
...  
Keyword(s):  
B Cells ◽  
Molecular Analysis ◽  
Combined Immunodeficiency ◽  
Gene Encoding ◽  
Clinical Phenotypes ◽  
Missense Allele ◽  
Complex Linear ◽  
Clinical Description ◽  
And Function

Inherited, complete deficiency of human HOIL-1, a component of the linear ubiquitination chain assembly complex (LUBAC), underlies autoinflammation, infections, and amylopectinosis. We report the clinical description and molecular analysis of a novel inherited disorder of the human LUBAC complex. A patient with multiorgan autoinflammation, combined immunodeficiency, subclinical amylopectinosis, and systemic lymphangiectasia, is homozygous for a mutation in HOIP, the gene encoding the catalytic component of LUBAC. The missense allele (L72P, in the PUB domain) is at least severely hypomorphic, as it impairs HOIP expression and destabilizes the whole LUBAC complex. Linear ubiquitination and NF-κB activation are impaired in the patient’s fibroblasts stimulated by IL-1β or TNF. In contrast, the patient’s monocytes respond to IL-1β more vigorously than control monocytes. However, the activation and differentiation of the patient’s B cells are impaired in response to CD40 engagement. These cellular and clinical phenotypes largely overlap those of HOIL-1-deficient patients. Clinical differences between HOIL-1- and HOIP-mutated patients may result from differences between the mutations, the loci, or other factors. Our findings show that human HOIP is essential for the assembly and function of LUBAC and for various processes governing inflammation and immunity in both hematopoietic and nonhematopoietic cells.

A Peruvian patient carrying the novel RHCE * cE ( c.382G > C ) missense allele in the RH blood group system

Transfusion ◽  
2021 ◽  
Author(s):  
Rémi Beloeil ◽  
Christine Guerry ◽  
Laurence Le Glatin ◽  
Charlotte Magdelaine ◽  
Audrey Dieudonné ◽  
...  
Keyword(s):  
Blood Group ◽  
Blood Group System ◽  
The Novel ◽  
Group System ◽  
Missense Allele ◽  
Rh Blood Group

scholarly journals PanR1, a Dominant Negative Missense Allele of the Gene Encoding TNF-α (Tnf), Does Not Impair Lymphoid Development

2006 ◽  
Vol 176 (12) ◽  
pp. 7525-7532 ◽  
Author(s):  
Sophie Rutschmann ◽  
Kasper Hoebe ◽  
Jonathan Zalevsky ◽  
Xin Du ◽  
Navjiwan Mann ◽  
...  
Keyword(s):  
Dominant Negative ◽  
Gene Encoding ◽  
Lymphoid Development ◽  
Tnf Α ◽  
Missense Allele

scholarly journals Mutation of the ER retention receptor KDELR1 leads to cell-intrinsic lymphopenia and a failure to control chronic viral infection

2015 ◽  
Vol 112 (42) ◽  
pp. E5706-E5714 ◽  
Author(s):  
Owen M. Siggs ◽  
Daniel L. Popkin ◽  
Philippe Krebs ◽  
Xiaohong Li ◽  
Miao Tang ◽  
...  
Keyword(s):  
Viral Infection ◽  
Mhc Class I ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Chronic Viral Infection ◽  
Protein Retention ◽  
C Terminus ◽  
Er Retention ◽  
Missense Allele ◽  
Kdel Receptor

Endoplasmic reticulum (ER)-resident proteins are continually retrieved from the Golgi and returned to the ER by Lys-Asp-Glu-Leu (KDEL) receptors, which bind to an eponymous tetrapeptide motif at their substrate's C terminus. Mice and humans possess three paralogous KDEL receptors, but little is known about their functional redundancy, or if their mutation can be physiologically tolerated. Here, we present a recessive mouse missense allele of the prototypical mammalian KDEL receptor, KDEL ER protein retention receptor 1 (KDELR1).Kdelr1homozygous mutants were mildly lymphopenic, as were mice with a CRISPR/Cas9-engineered frameshift allele. Lymphopenia was cell intrinsic and, in the case of T cells, was associated with reduced expression of the T-cell receptor (TCR) and increased expression of CD44, and could be partially corrected by an MHC class I-restricted TCR transgene. Antiviral immunity was also compromised, withKdelr1mutant mice unable to clear an otherwise self-limiting viral infection. These data reveal a nonredundant cellular function for KDELR1, upon which lymphocytes distinctly depend.

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