3 research outputs found
Coaching the quiet: Exploring coaches’ beliefs about shy children in a sport context
Organized sports may enhance the social skills and peer relationships of shy children. Interactions with coaches may be critical determinants of these benefits. Thus, our goal was to explore coaches’ beliefs, attitudes, and responses to shy children. Participants were 447 undergraduate students (343 female; Mage = 19.39 years, SD = 2.12) with coaching experience. Participants indicated their anticipated behaviours, emotions, and perceived implications in response to hypothetical children exhibiting shy, unsociable, and verbally exuberant behaviours in a sport context. Coaches viewed shy behaviour more problematically than both verbally exuberant and unsociable behaviours, anticipating the most negative implications for shy children's peer relationships, development, and team performance and supporting the use of differential coaching strategies. However, despite reporting the most worry about shyness, coaches were less likely to intervene in response to shyness compared to exuberance. We discuss the implications that our results may have for the adjustment of shy children
The fragile X-related proteins FXR1P and FXR2P contain a functional nucleolar-targeting signal equivalent to the HIV-1 regulatory proteins
Fragile X syndrome is caused by the absence of the fragile X
mental-retardation protein (FMRP). FMRP and the fragile X-related proteins
1 and 2 (FXR1P and FXR2P) form a gene family with functional similarities,
such as RNA binding, polyribosomal association and nucleocytoplasmic
shuttling. In a previous study, we found that FMRP and FXR1P shuttle
between cytoplasm and nucleoplasm, while FXR2P shuttles between cytoplasm
and nucleolus. The nuclear and nucleolar-targeting properties of these
proteins were investigated further. Here, we show that FXR2P contains in
its C-terminal part, a stretch of basic amino acids 'RPQRRNRSRRRRFR' that
resemble the nucleolar-targeting signal (NoS) of the viral protein Rev.
This particular sequence is also present within exon 15 of the FXR1 gene.
This exon undergoes alternative splicing and is therefore only present in
some of the FXR1P isoforms. We investigated the intracellular distribution
of various FXR1P isoforms with (iso-e and iso-f) and without (iso-d) the
potential NoS in transfected COS cells treated with the nuclear export
inhibitor leptomycin-B. Both iso-e and iso-f showed a nucleolar
localization, as observed for FXR2P; iso-d was detected in the
nucleo-plasm outside the nucleoli. Further, when a labelled 16-residue
synthetic peptide corresponding to the NoS of FXR1P was added to human
fibroblast cultures a clear nucleolar signal was observed. Based on these
data we argue that the intranuclear distribution of FXR2P and FXR1P
isoforms is very likely to be mediated by a similar NoS localized in their
C-terminal region. This domain is absent in some FXR1P isoforms as well as
in all FMRP isoforms, suggesting functional differences for this family of
proteins, possibly related to RNA metabolism in different tissues
Fxr1 knockout mice show a striated muscle phenotype: implications for Fxr1p function in vivo.
FXR1 is one of the two known homologues of FMR1. FXR1 shares a high degree
of sequence homology with FMR1 and also encodes two KH domains and an RGG
domain, conferring RNA-binding capabilities. In comparison with FMRP, very
little is known about the function of FXR1P in vivo. Mouse knockout (KO)
models exist for both Fmr1 and Fxr2. To study the function of Fxr1 in
vivo, we generated an Fxr1 KO mouse model. Homozygous Fxr1 KO neonates die
shortly after birth most likely due to cardiac or respiratory failure.
Histochemical analyses carried out on both skeletal and cardiac muscles
show a disruption of cellular architecture and structure in E19 Fxr1
neonates compared with wild-type (WT) littermates. In WT E19 skeletal and
cardiac muscles, Fxr1p is localized to the costameric regions within the
muscles. In E19 Fxr1 KO littermates, in addition to the absence of Fxr1p,
costameric proteins vinculin, dystrophin and alpha-actinin were found to
be delocalized. A second mouse model (Fxr1 + neo), which expresses
strongly reduced levels of Fxr1p relative to WT littermates, does not
display the neonatal lethal phenotype seen in the Fxr1 KOs but does
display a strongly reduced limb musculature and has a reduced life span of
approximately 18 weeks. The results presented here point towards a role
for Fxr1p in muscle mRNA transport/translation control similar to that
seen for Fmrp in neuronal cells