Cerebellar Ataxia, Cayman Type

Last update 08 May 2025

Basic Info

Synonyms

ATCAY, CAYMAN ATAXIA, CEREBELLAR ATAXIA, CAYMAN TYPE

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Introduction

Cerebellar ataxia Cayman type has characteristics of psychomotor retardation, hypotonia and cerebellar dysfunction (nystagmus, ataxic gait, truncal ataxia, dysarthric speech and intention tremor), associated with cerebellar hypoplasia. The prevalence is unknown, but the disorder is very rare in the general population. However, a founder mutation has led to a high incidence in the Cayman island population. The disorder is transmitted as an autosomal recessive trait and is caused by mutations in the ATCAY gene (19p13.3), encoding Caytaxin.

Clinical Trials associated with Cerebellar Ataxia, Cayman Type

NCT01793168

/ RecruitingNot Applicable

Coordination of Rare Diseases at Sanford

CoRDS, or the Coordination of Rare Diseases at Sanford, is based at Sanford Research in Sioux Falls, South Dakota. It provides researchers with a centralized, international patient registry for all rare diseases. This program allows patients and researchers to connect as easily as possible to help advance treatments and cures for rare diseases. The CoRDS team works with patient advocacy groups, individuals and researchers to help in the advancement of research in over 7,000 rare diseases. The registry is free for patients to enroll and researchers to access. Visit sanfordresearch.org/CoRDS to enroll.

Start Date01 Jul 2010

Sponsor / Collaborator

Sanford Health Corp.

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100 Clinical Results associated with Cerebellar Ataxia, Cayman Type

100 Translational Medicine associated with Cerebellar Ataxia, Cayman Type

0 Patents (Medical) associated with Cerebellar Ataxia, Cayman Type

Literatures (Medical) associated with Cerebellar Ataxia, Cayman Type

01 Jun 2018·Brain ResearchQ4 · MEDICINE

Odor preference and olfactory memory are impaired in Olfaxin-deficient mice

Q4 · MEDICINE

Article

Author: Lee, Dongsoo ; Nakagawa, Toshiyuki ; Islam, Saiful ; Ueda, Masashi ; Wang, Miao-Xing ; Itoh, Masanori ; Nakagawa, Kiyomi ; Osawa, Masatake ; Tana ; Nishida, Emika

Olfaxin, which is a BNIP2 and Cdc42GAP homology (BCH) domain-containing protein, is predominantly expressed in mitral and tufted (M/T) cells in the olfactory bulb (OB). Olfaxin and Caytaxin, which share 56.3% amino acid identity, are similar in their glutamatergic terminal localization, kidney-type glutaminase (KGA) interaction, and caspase-3 substrate. Although the deletion of Caytaxin protein causes human Cayman ataxia and ataxia in the mutant mouse, the function of Olfaxin is largely unknown. In this study, we generated Prune2 gene mutant mice (Prune2^Ex16-/-; knock out [KO] mice) using the CRISPR/Cas9 system, during which the exon 16 containing start codon of Olfaxin mRNA was deleted. Exon 16 has 80 nucleotides and is contained in four of five Prune2 isoforms, including PRUNE2, BMCC1, BNIPXL, and Olfaxin/BMCC1s. The levels of Olfaxin mRNA and Olfaxin protein in the OB and piriform cortex of KO mice significantly decreased. Although Prune2 mRNA also significantly decreased in the spinal cord, the gross anatomy of the spinal cord and dorsal root ganglion (DRG) was intact. Further, disturbance of the sensory and motor system was not observed in KO mice. Therefore, in the current study, we examined the role of Olfaxin in the olfactory system where PRUNE2, BMCC1, and BNIPXL are scarcely expressed. Odor preference was impaired in KO mice using opposite-sex urinary scents as well as a non-social odor stimulus (almond). Results of the odor-aversion test demonstrated that odor-associative learning was disrupted in KO mice. Moreover, the NMDAR2A/NMDAR2B subunits switch in the piriform cortex was not observed in KO mice. These results indicated that Olfaxin may play a critical role in odor preference and olfactory memory.

01 Feb 2015·Genes to CellsQ4 · BIOLOGY

BNIP‐2 binds phosphatidylserine, localizes to vesicles, and is transported by kinesin‐1

Q4 · BIOLOGY

Article

Author: Akamatsu, Rie ; Oka, Chio ; Aoyama, Takane ; Ishida‐Kitagawa, Norihiro ; Kawaichi, Masashi

BNIP‐2 shows high homology with the Cayman ataxia protein, caytaxin, which functions as a kinesin‐1 adapter bridging cargos and kinesin light chains (KLCs). BNIP‐2 is known to induce cell shape changes when over‐expressed in culture cells, but its physiological functions are mostly unknown. BNIP‐2 interacts with KLC through the conserved WED motif in the N‐terminal region of BNIP‐2. Interaction with KLC and transportation by kinesin‐1 are essential for over‐expressed BNIP‐2 to elongate cells and induce cellular processes. Endogenous BNIP‐2 localizes to the Golgi apparatus, early and recycling endosomes and mitochondria, aligned with microtubules, and moves at a speed compatible with kinesin‐1 transportation. The CRAL–TRIO domain of BNIP‐2 specifically interacts with phosphatidylserine, and the vesicular localization of BNIP‐2 requires interaction with this phospholipid. BNIP‐2 mutants which do not bind phosphatidylserine do not induce morphological changes in cells. These data show that similar to caytaxin, BNIP‐2 is a kinesin‐1 adapter involved in vesicular transportation in the cytoplasm and that association with cargos depends on interaction of the CRAL–TRIO domain with membrane phosphatidylserine.

01 Jul 2011·Neurochemical ResearchQ3 · MEDICINE

Cayman Ataxia-Related Protein is a Presynapse-Specific Caspase-3 Substrate

Q3 · MEDICINE

Article

Author: Masanori Itoh ; Yoshiko Banno ; Masashi Ueda ; Eri Ohta ; Akihito Mizuno ; Yoshika Hayakawa-Yano ; Yoshihiro Suzuki ; Shimo Li ; Toshiyuki Nakagawa ; Kazunori Ohta ; Yoko Hida ; Aiko Yamada

Caspase plays an important role in apoptosis and physiological processes such as synaptic plasticity. However, the caspase substrate at the synapse is still unknown. Here we used an in vitro cleavage assay with a small-pool human brain cDNA library. We identified the presynaptic protein Caytaxin as a substrate of caspase-3 and caspase-7. Deficiency in Caytaxin causes Cayman ataxia, a disorder characterized by cerebellar dysfunction and mental retardation. Caytaxin cleavage in cerebellar granule neurons is dependent on caspase-3 activation. The cleavage site is upstream of the cellular retinal and the TRIO guanine exchange factor domain, producing a C-terminal fragment that may play an alternative role in inhibiting MEK2 signaling. Thus, we concluded that Caytaxin is a novel substrate of caspase-3 at the presynapse.

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