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J Biol Chem, Vol. 273, Issue 12, 6591-6594, March 20, 1998
From the Department of Molecular Biology and Biochemistry, Osaka
University Medical School, Suita 565, Japan
We have recently isolated SMAP (Smg
GDS-associated protein; Smg GDS:
small G protein GDP
dissociation stimulator) as a novel Smg
GDS-associated protein, which has Armadillo repeats and is phosphorylated by Src tyrosine kinase. SMAP is a human counterpart of
mouse KAP3 (kinesin superfamily-associated
protein) that is associated with mouse KIF3A/B (a
kinesin superfamily protein), which functions
as a microtubule-based ATPase motor for organelle transport. We
isolated here a SMAP-interacting protein from a human brain cDNA
library, identified it to be a human homolog of Xenopus
XCAP-E (Xenopus
chromosome-associated polypeptide), a subunit of condensins that regulate the assembly and structural maintenance of mitotic chromosomes, and named it HCAP
(Human chromosome-associated polypeptide). Tissue and subcellular distribution analyses
indicated that HCAP was ubiquitously expressed and highly concentrated
in the nuclear fraction, where SMAP and KIF3B were also present. SMAP
was extracted as a ternary complex with HCAP and KIF3B from the nuclear
fraction in the presence of Mg-ATP. The results suggest that SMAP/KAP3
serves as a linker between HCAP and KIF3A/B in the nucleus, and that
SMAP/KAP3 plays a role in the interaction of chromosomes with an ATPase
motor protein.
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