@article {635,
	title = {Recessive coding and regulatory mutations in FBLIM1 underlie the pathogenesis of chronic recurrent multifocal osteomyelitis (CRMO).},
	journal = {PLoS One},
	volume = {12},
	year = {2017},
	month = {2017},
	pages = {e0169687},
	abstract = {<p>Chronic recurrent multifocal osteomyelitis (CRMO) is a rare, pediatric, autoinflammatory disease characterized by bone pain due to sterile osteomyelitis, and is often accompanied by psoriasis or inflammatory bowel disease. There are two syndromic forms of CRMO, Majeed syndrome and DIRA, for which the genetic cause is known. However, for the majority of cases of CRMO, the genetic basis is unknown. Via whole-exome sequencing, we detected a homozygous mutation in the filamin-binding domain of FBLIM1 in an affected child with consanguineous parents. Microarray analysis of bone marrow macrophages from the CRMO murine model (cmo) determined that the Fblim1 ortholog is the most differentially expressed gene, downregulated over 20-fold in the cmo mouse. We sequenced FBLIM1 in 96 CRMO subjects and found a second proband with a novel frameshift mutation in exon 6 and a rare regulatory variant. In SaOS2 cells, overexpressing the regulatory mutation showed the flanking region acts as an enhancer, and the mutation ablates enhancer activity. Our data implicate FBLIM1 in the pathogenesis of sterile bone inflammation and our findings suggest CRMO is a disorder of chronic inflammation and imbalanced bone remodeling.</p>},
	keywords = {Amino Acid Sequence, Animals, Cell Adhesion Molecules, Cell Line, Tumor, Child, Cytoskeletal Proteins, Female, Genes, Recessive, Humans, Interleukin-10, Mice, Mutation, Osteomyelitis, Promoter Regions, Genetic, Sequence Homology, Amino Acid},
	issn = {1932-6203},
	doi = {10.1371/journal.pone.0169687},
	author = {Cox, Allison J and Darbro, Benjamin W and Laxer, Ronald M and Velez, Gabriel and Bing, Xinyu and Finer, Alexis L and Erives, Albert and Mahajan, Vinit B and Bassuk, Alexander G and Ferguson, Polly J}
}
@article {831,
	title = {Connectin: a homophilic cell adhesion molecule expressed on a subset of muscles and the motoneurons that innervate them in Drosophila.},
	journal = {Cell},
	volume = {70},
	year = {1992},
	month = {1992 Aug 21},
	pages = {553-67},
	abstract = {<p>Each abdominal hemisegment in the Drosophila embryo contains a stereotyped array of 30 muscles, each specifically innervated by one or a few motoneurons. We screened 11,000 enhancer trap lines, isolated several expressing beta-galactosidase in small subsets of muscle fibers prior to innervation, and identified two of these as inserts in connectin and Toll, members of the leucine-rich repeat gene family. Connectin contains a signal sequence, ten leucine-rich repeats, and a putative phosphatidylinositol membrane linkage; in S2 cells, connectin can mediate homophilic cell adhesion. Connectin is expressed on the surface of eight muscles, the motoneurons that innervate them, and several glial cells along the pathways leading to them. During synapse formation, the protein localizes to synaptic sites; afterward, it largely disappears. Thus, connectin is a novel cell adhesion molecule whose expression suggests a role in target recognition.</p>
},
	keywords = {Amino Acid Sequence, Animals, Base Sequence, Cell Adhesion Molecules, Cloning, Molecular, Connectin, DNA, Drosophila, Molecular Sequence Data, Motor Neurons, Muscle Proteins, Muscles, Protein Kinases, Sequence Alignment},
	issn = {0092-8674},
	author = {Nose, A and Mahajan, V B and Goodman, C S}
}
