Cytoskeletal Cytoplasmic Filament Ribbon of Treponema: A Member of an Intermediate-Like Filament Protein Family

2006 ◽  
Vol 11 (3-5) ◽  
pp. 159-166 ◽  
Author(s):  
Jacques Izard
Keyword(s):  
Protein Family ◽  
Cytoplasmic Filament ◽  
Filament Protein

scholarly journals Characterization of the cytoplasmic filament protein gene (cfpA) of Treponema pallidum subsp. pallidum.

1996 ◽  
Vol 178 (11) ◽  
pp. 3177-3187 ◽  
Author(s):  
Y You ◽  
S Elmore ◽  
L L Colton ◽  
C Mackenzie ◽  
J K Stoops ◽  
...  
Keyword(s):  
Protein Gene ◽  
Treponema Pallidum ◽  
Cytoplasmic Filament ◽  
Filament Protein

Peripherin, a New Member of the Intermediate Filament Protein Family

1983 ◽  
Vol 6 (6) ◽  
pp. 335-344 ◽  
Author(s):  
Marie-Madeleine Portier ◽  
Béatrice de Néchaud ◽  
François Gros
Keyword(s):  
Intermediate Filament ◽  
Protein Family ◽  
Intermediate Filament Protein ◽  
Filament Protein

scholarly journals Molecular cloning of a gene (cfp) encoding the cytoplasmic filament protein P59Nc and its genetic relationship to the snowflake locus of Neurospora crassa.

Genetics ◽  
1992 ◽  
Vol 131 (3) ◽  
pp. 575-580
Author(s):  
S D Haedo ◽  
E D Temporini ◽  
M E Alvarez ◽  
H J Maccioni ◽  
A L Rosa
Keyword(s):  
Neurospora Crassa ◽  
Molecular Cloning ◽  
Genetic Locus ◽  
Restriction Enzymes ◽  
Genomic Region ◽  
Total Dna ◽  
Cytoplasmic Filament ◽  
The Right ◽  
Filament Protein ◽  
Chromosome I

Abstract P59Nc is a 59-kD polypeptide associated with 8-10-nm diameter cellular filaments in normal Neurospora crassa strains. Abnormally sized and shaped bundles of these structures are present in N. crassa strains carrying mutations at the locus sn (snowflake). By using molecular cloning and restriction fragment length polymorphism (RFLP) segregation analysis strategies we show here that sn is not the genetic locus of P59Nc. Several P59Nc cDNAs were cloned from a N. crassa lambda GT11 library after immunoscreening with specific polyclonal anti-P59Nc antibodies. Additional longer cDNAs were obtained from a N. crassa cDNA-lambda ZAP library. When used as probes in Southern blots of total DNA from wild-type strains, multicent-2 (a multiple mutant strain), and snowflake mutants, the P59Nc cDNAs revealed comparable patterns of hybridizing bands for all of the restriction enzymes tested. Analysis of segregation of BclI and ClaI RFLPs, detected in the genomic region of the P59Nc gene (locus cfp: cellular filament polypeptide), among a set of strains designed for RFLP mapping, or among selected progeny of crosses involving a snowflake parent, respectively, indicate that (i) there is in N. crassa a single cfp locus positioned on the right arm of linkage group VII between the locus for and the proximal breakpoint of the translocation T(VII----I)5936; (ii) the sn mutations in the centromere region of chromosome I do not represent translocations of cfp; and (iii) the snowflake mutants possesses a normal copy of the P59Nc gene on their chromosomes VII.(ABSTRACT TRUNCATED AT 250 WORDS)

Immunocytochemical localization of desmin and vimentin in chick embryonic myocardial cells

1990 ◽  
Vol 48 (3) ◽  
pp. 448-449
Author(s):  
Yukiko Sugi
Keyword(s):  
Sodium Methoxide ◽  
Intermediate Filament Protein ◽  
Chick Embryos ◽  
Immunocytochemical Localization ◽  
Myocardial Cells ◽  
Immunofluorescence Study ◽  
Immunofluorescent Localization ◽  
Rabbit Igg ◽  
Semithin Sections ◽  
Filament Protein

In cultured skeletal muscle cells of chick, one intermediate filament protein, vimentin, is primarily formed and then synthesis of desmin follows. Coexistence of vimentin and desmin has been immunocytochemically confirmed in chick embryonic skeletal musclecells. Immunofluorescent localization of vimentin and desmin has been described in developing myocardial cells of hamster. However, initial localization of desmin and vimentin in early embryonic heart has not been reported in detail. By quick-freeze deep-etch method a loose network of intermediate filaments was revealed to exist surrounding myofibrils. In this report, immunocytochemical localization of desmin and vimentin is visualized in early stages of chick embryonic my ocardium.Chick embryos, Hamburger-Hamilton (H-H) stage 8 to hatch, and 1 day old postnatal chicks were used in this study. For immunofluorescence study, each embryo was fixed with 4% paraformaldehyde and embedded in Epon 812. De-epoxinized with sodium methoxide, semithin sections were stained with primary antibodies (rabbit anti-desmin antibody and anti-vimentin antibody)and secondary antibody (RITC conjugated goat-anti rabbit IgG).

Investigating the functional link between TMEM165 and SPCA1

2019 ◽  
Vol 476 (21) ◽  
pp. 3281-3293 ◽  
Author(s):  
Elodie Lebredonchel ◽  
Marine Houdou ◽  
Hans-Heinrich Hoffmann ◽  
Kateryna Kondratska ◽  
Marie-Ange Krzewinski ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Complete Loss ◽  
Protein Family ◽  
Uncharacterized Protein ◽  
Functional Link ◽  
P Type

TMEM165 was highlighted in 2012 as the first member of the Uncharacterized Protein Family 0016 (UPF0016) related to human glycosylation diseases. Defects in TMEM165 are associated with strong Golgi glycosylation abnormalities. Our previous work has shown that TMEM165 rapidly degrades with supraphysiological manganese supplementation. In this paper, we establish a functional link between TMEM165 and SPCA1, the Golgi Ca2+/Mn2+ P-type ATPase pump. A nearly complete loss of TMEM165 was observed in SPCA1-deficient Hap1 cells. We demonstrate that TMEM165 was constitutively degraded in lysosomes in the absence of SPCA1. Complementation studies showed that TMEM165 abundance was directly dependent on SPCA1's function and more specifically its capacity to pump Mn2+ from the cytosol into the Golgi lumen. Among SPCA1 mutants that differentially impair Mn2+ and Ca2+ transport, only the Q747A mutant that favors Mn2+ pumping rescues the abundance and Golgi subcellular localization of TMEM165. Interestingly, the overexpression of SERCA2b also rescues the expression of TMEM165. Finally, this paper highlights that TMEM165 expression is linked to the function of SPCA1.

The involvement of the GGA protein family in BACE transport and APP processing in Alzheimer's disease

2008 ◽  
Vol 35 (S 01) ◽  
Author(s):  
C Steinmetz ◽  
B von Einem ◽  
D Schwanzar ◽  
F Dolp ◽  
A.C Ludolph ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Family ◽  
App Processing
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