Synaptotagmin genes on mouse Chromosomes 1, 7, and 10 and human Chromosome 19

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/47020/1/335_2004_Article_BF00293017.pd

Localization of the murine cholecystokinin A and B receptor genes

We have determined the chromosomal locations of the two cholecystokinin (CCK) receptor genes in the mouse. Genetic localization utilized an interspecific backcross panel formed from the cross (C57BL/6J x Mus spretus ) F 1 x Mus spretus . Genomic DNAs from 94 individuals in the backcross were analyzed by Southern hybridization with rat CCK A and CCK B receptor cDNA probes. Unique map positions were determined by haplotype analysis with 650 previously mapped loci in the mouse backcross. The CCK A receptor gene ( Cckar ) mapped to mouse Chromosome (Chr) 5, in tight linkage with the DNA marker D5Bir8 . The CCK B receptor gene ( Cckbr ) mapped to mouse Chr 7, tightly linked to the β-hemoglobin locus ( Hbb ). This localization places Cckbr in the same region as the mouse obesity mutation tubby ( tub ), which also maps near Hbb (2.4±1.4 cM). Since CCK can function as a satiety factor when administered to rodents, localization of Cckbr near the tub mutation identifies this receptor as a possible candidate gene for this obesity mutation.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/47021/1/335_2004_Article_BF00352408.pd

The co-repressor mSin3A is a functional component of the REST-CoREST repressor complex

The repressor REST/NRSF restricts expression of a large set of genes to neurons by suppressing their expression in non-neural tissues. We find that REST repression involves two distinct repressor proteins. One of these, CoREST, interacts with the COOH-terminal repressor domain of REST (Andres, M. E., Burger, C., Peral-Rubio, M. J., Battaglioli, E., Anderson, M. E., Grimes, J., Dallmanm J., Ballas, N., and Mandel, G. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 9873-9878). Here we show that the co-repressor mSin3A also interacts with REST. The REST-mSin3A association involves the NH2-terminal repressor domain of REST and the paired amphipathic helix 2 domain of mSin3A. REST forms complexes with endogenous mSin3A in mammalian cells, and both mSin3A and CoREST interact with REST in intact mammalian cells. REST repression is blocked in yeast lacking Sin3 and rescued in its presence. In mammalian cells, repression by REST is reduced when binding to mSin3A is inhibited. In mouse embryos, the distribution of mSin3A and REST transcripts is largely coincident. The pattern of CoREST gene expression is more restricted, suggesting that mSin3A is required constitutively for REST repression, whereas CoREST is recruited for more specialized repressor functions