Psychiatry related information on Kifap3

• In addition, we found that KAP3 does not affect the motor activity of KIF3A/3B [1].

High impact information on Kifap3

• Furthermore, in KAP3-deficient cells, the subcellular localization of N-cadherin was disrupted [2].
• Moreover, we found that the composition of KAP3 is different in the brain and testis [3].
• KAP3 was associated with a membrane-bound form of KIF3A/3B in a fractional immunoprecipitation experiment, and since the KIF3 complex was found to bind to membranous organelles in an EM study, KAP3 may regulate membrane binding of the KIF3 complex [1].
• Microsequencing was carried out, and we cloned the full-length KAP3 cDNA from a mouse brain cDNA library [1].
• The immunolocalization pattern of KAP3 was similar to that of KIF3A/3B in nerve cells [1].

Biological context of Kifap3

• Two isoforms of KAP3 exist [KAP3A (793 aa) and KAP3B (772 aa)], generated by alternative splicing in the carboxyl terminus region [1].
• Their amino acid sequences have no homology with those of any other known proteins, and prediction of their secondary structure indicated that almost the entire KAP3 molecule is alpha-helical [1].
• Smg GDS-/- thymocytes were protected from etoposide-induced cell death by ex vivo transduction of the Smg GDS cDNA [4].
• Here we show that mice lacking Smg GDS died of heart failure shortly after birth, not resulting from developmental heart defects but from enhanced apoptosis of cardiomyocytes triggered by cardiovascular overload [4].
• These phenotypes partly coincide with those observed in Ki-Ras-deficient mice, suggesting that Smg GDS is involved in antiapoptotic cell survival signaling through Ki-Ras [4].

Anatomical context of Kifap3

• In the present study, we purified KAP3 protein by immunoprecipitation using anti-KIF3B antibody from mouse testis [1].
• In fibroblasts, Smg GDS shows mitogenic and transforming activities in cooperation with Ki-Ras [4].
• Small GTP-binding protein GDP dissociation stimulator (Smg GDS) regulates GDP/GTP exchange reaction of Ki-Ras and the Rho and Rap1 family members and inhibits their binding to membranes [4].
• Immunohistochemical studies further revealed that KAP3 protein predominantly accumulates in large motor neurons of the ventral spinal cord [5].
• Fifteen clones such as clone 7-3 showed no match in the GenBank Database. Further characterization of eight clones (17-1, 7-3, 8-1, 5-1, NELL2, KAP3 homolog, IgE binding lectin homolog, and TTF-1) showed that their expression in the adult female rat hypothalamus is sensitive to neonatal treatment with EB [6].

Analytical, diagnostic and therapeutic context of Kifap3

• RT-PCR analysis revealed that KAP3 induction was an early event arising long before axonal degeneration [5].
• Using an optimized suppression subtractive hybridization method, a cDNA specifically up-regulated during the asymptomatic phase in the lumbar spinal cord of G86R mice was identified by sequence analysis as the KIF3-associated protein (KAP3), a regulator of fast axonal transport [5].

References