Genomic organization, expression profile, and characterization of the new protein PRA1 domain family, member 2 (PRAF2)

Fo, Crystal S.; Coleman, Craig S.; Wallick, Christopher J.; Vine, Alex L.; Bachmann, André S.

doi:10.1016/j.gene.2005.12.009

Cited by 31 publications

(50 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Regarding the spatial distribution, PRA1 homologs have been ubiquitously found in human tissues, emphasizing their importance for development (Martincic et al, 1997;Abdul-Ghani et al, 2001;Bucci et al, 2001;Schweneker et al, 2005;Fo et al, 2006). Based on our results in 8-d-old seedlings, AtPRA1 transcripts are differently distributed, mainly accumulating in emerging organs and vascular tissues.…”

Section: Discussionsupporting

confidence: 51%

ThePRA1Gene Family in Arabidopsis

Kamei

Boruc²,

Vandepoele³

et al. 2008

Plant Physiology

View full text Add to dashboard Cite

Prenylated Rab acceptor 1 (PRA1) domain proteins are small transmembrane proteins that regulate vesicle trafficking as receptors of Rab GTPases and the vacuolar soluble N-ethylmaleimide-sensitive factor attachment receptor protein VAMP2. However, little is known about PRA1 family members in plants. Sequence analysis revealed that higher plants, compared with animals and primitive plants, possess an expanded family of PRA1 domain-containing proteins. The Arabidopsis (Arabidopsis thaliana) PRA1 (AtPRA1) proteins were found to homodimerize and heterodimerize in a manner corresponding to their phylogenetic distribution. Different AtPRA1 family members displayed distinct expression patterns, with a preference for vascular cells and expanding or developing tissues. AtPRA1 genes were significantly coexpressed with Rab GTPases and genes encoding vesicle transport proteins, suggesting an involvement in the vesicle trafficking process similar to that of their animal counterparts. Correspondingly, AtPRA1 proteins were localized in the endoplasmic reticulum, Golgi apparatus, and endosomes/ prevacuolar compartments, hinting at a function in both secretory and endocytic intracellular trafficking pathways. Taken together, our data reveal a high functional diversity of AtPRA1 proteins, probably dealing with the various demands of the complex trafficking system.

show abstract

Section: Discussionsupporting

confidence: 51%

ThePRA1Gene Family in Arabidopsis

Kamei

Boruc²,

Vandepoele³

et al. 2008

Plant Physiology

View full text Add to dashboard Cite

show abstract

“…For assays, an aliquot was thawed, and 3 AL cerulenin/ mL of cell culture medium were added (final concentration, 15 Ag/mL). The PRAF2 polyclonal rabbit peptide antibody and the peptide preblocked PRAF2 antibody (PRAF2-P; control) were described before (6) and are available from QED Bioscience. PRAF2 and PRAF2-P antibodies were used at a final concentration of 0.6 Ag/mL.…”

Section: Methodsmentioning

confidence: 99%

“…Cell lysates were prepared as previously reported (12) using radioimmunoprecipitation assay buffer [20 mmol/L Tris-HCl (pH 7.5), 0.1% (w/v) sodium lauryl sulfate, 0.5% (w/v) sodium deoxycholate, 135 mmol/L NaCl, 1% (v/v) Triton X-100, 10% (v/v) glycerol, 2 mmol/L EDTA], supplemented with complete protease inhibitor cocktail (Roche Molecular Biochemicals), phosphatase inhibitors sodium fluoride (NaF; 20 mmol/L), and sodium vanadate (Na 3 VO 4 ; 0.27 mmol/L). SDS-PAGE and electrotransfer to polyvinylidene difluoride Immobilon-P membrane (Millipore) was done as previously described (6). Membranes were blocked in Blotto buffer [50 mmol/L Tris-HCl (pH 7.5), 150 mmol/L NaCl, 0.1% (v/v) Triton X-100, supplemented with 5% (w/v) nonfat dry milk from Santa Cruz Biotechnology (Santa Cruz)] for 1 h at room temperature.…”

Section: Methodsmentioning

confidence: 99%

“…23, and the PRAF2 protein is present in many human tissues with high expression in the brain (6). Most intriguingly, our previous studies revealed that PRAF2 is overexpressed in human cancer tissues of the breast, colon, lung, and ovary with a weaker presence in normal tissues of paired samples from a tissue microarray (6). PRAF2 interacts with chemokine receptor CCR5 (7) and human glycerophosphoinositol phosphodiesterase GDE1/MIR16 (8).…”

mentioning

confidence: 98%

“…Prenylated Rab acceptor 1 domain family, member 2 (PRAF2; previously designated JM4) is a recently identified 19-kDa protein with a prenylated Rab acceptor motif and four transmembrane domains (6,7). The human PRAF2 gene is located on chromosome Xp11.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Expression of Prenylated Rab Acceptor 1 Domain Family, Member 2 (PRAF2) in Neuroblastoma: Correlation with Clinical Features, Cellular Localization, and Cerulenin-Mediated Apoptosis Regulation

Geerts

Wallick

Koomoa

et al. 2007

Clinical Cancer Research

Self Cite

View full text Add to dashboard Cite

Purpose: Prenylated Rab acceptor1domain family, member 2 (PRAF2) is a novel 19-kDa protein that has recently been implicated in human cancer. In the present study, we analyzed for the first time PRAF2 mRNA expression in a large set of human tumors.The high expression in neuroblastic tumors prompted us to analyze PRAF2 expression correlations with genetic and clinical features of these tumors. In addition, we determined the localization of PRAF2 protein in neuroblastoma cells and studied its regulation in apoptosis. Experimental Design: Affymetrix microarray analysis was done with a set of 41different tumor types (1,426 samples) in the public domain, a set of three different neuroblastic tumor types (110 samples), and a panel of 25 neuroblastoma cell lines. The subcellular localization of endogenous PRAF2 in neuroblastoma cells was identified by immunofluorescence microscopy and apoptosis detected by AnnexinV staining and poly(ADP-ribose) polymerase cleavage. Results: PRAF2 mRNA was detected in 970 of 1,426 samples in the public data set. All 110 neuroblastic tumors expressed PRAF2 at higher levels than any other tumor examined. Importantly, PRAF2 expression levels significantly correlated with the following clinical features: patient age at diagnosis (P = 6.19 Â 10 -5

show abstract

Phenotype–genotype correlations in 17 new patients with an Xp11.23p11.22 microduplication and review of the literature

Nizon

Andrieux

Rooryck

et al. 2014

American J of Med Genetics Pt A

View full text Add to dashboard Cite

Array comparative genomic hybridization (array CGH) has proven its utility in uncovering cryptic rearrangements in patients with X-linked intellectual disability. In 2009, Giorda et al. identified inherited and de novo recurrent Xp11.23p11.22 microduplications in two males and six females from a wide cohort of patients presenting with syndromic intellectual disability. To date, 14 females and 5 males with an overlapping microduplication have been reported in the literature. To further characterize this emerging syndrome, we collected clinical and microarray data from 17 new patients, 10 females, and 7 males. The Xp11.23p11.2 microduplications detected by array CGH ranged in size from 331 Kb to 8.9 Mb. Five patients harbored 4.5 Mb recurrent duplications mediated by non-allelic homologous recombination between segmental duplications and 12 harbored atypical duplications. The chromosomal rearrangement occurred de novo in eight patients and was inherited in six affected males from three families. Patients shared several common major characteristics including moderate to severe intellectual disability, early onset of puberty, language impairment, and age related epileptic syndromes such as West syndrome and focal epilepsy with activation during sleep evolving in some patients to continuous spikes-and-waves during slow sleep. Atypical microduplications allowed us to identify minimal critical regions that might be responsible for specific clinical findings of the syndrome and to suggest possible candidate genes: FTSJ1 and SHROOM4 for intellectual disability along with PQBP1 and SLC35A2 for epilepsy. Xp11.23p11.22 microduplication is a recently-recognized syndrome associated with intellectual disability, epilepsy, and early onset of puberty in females. In this study, we propose several genes that could contribute to the phenotype.

show abstract

Genomic organization, expression profile, and characterization of the new protein PRA1 domain family, member 2 (PRAF2)

Cited by 31 publications

References 29 publications

ThePRA1Gene Family in Arabidopsis

ThePRA1Gene Family in Arabidopsis

Expression of Prenylated Rab Acceptor 1 Domain Family, Member 2 (PRAF2) in Neuroblastoma: Correlation with Clinical Features, Cellular Localization, and Cerulenin-Mediated Apoptosis Regulation

Phenotype–genotype correlations in 17 new patients with an Xp11.23p11.22 microduplication and review of the literature

Contact Info

Product

Resources

About