scholarly journals Specific Sequences of the Sm and Sm-like (Lsm) Proteins Mediate Their Interaction with the Spinal Muscular Atrophy Disease Gene Product (SMN)

2000 ◽  
Vol 275 (34) ◽  
pp. 26370-26375 ◽  
Author(s):  
Westley John Friesen ◽  
Gideon Dreyfuss
Keyword(s):  
Spinal Muscular Atrophy ◽  
Gene Product ◽  
Disease Gene ◽  
Muscular Atrophy ◽  
Specific Sequences

scholarly journals A Novel Function for SMN, the Spinal Muscular Atrophy Disease Gene Product, in Pre-mRNA Splicing

Cell ◽  
1998 ◽  
Vol 95 (5) ◽  
pp. 615-624 ◽  
Author(s):  
Livio Pellizzoni ◽  
Naoyuki Kataoka ◽  
Bernard Charroux ◽  
Gideon Dreyfuss
Keyword(s):  
Spinal Muscular Atrophy ◽  
Gene Product ◽  
Disease Gene ◽  
Muscular Atrophy ◽  
Mrna Splicing

scholarly journals The Spinal Muscular Atrophy Disease Gene Product, Smn

1999 ◽  
Vol 147 (4) ◽  
pp. 715-728 ◽  
Author(s):  
Teresa Carvalho ◽  
Fátima Almeida ◽  
Alexandre Calapez ◽  
Miguel Lafarga ◽  
Maria T. Berciano ◽  
...  
Keyword(s):  
Spinal Muscular Atrophy ◽  
Gene Product ◽  
Disease Gene ◽  
Cultured Cells ◽  
Muscular Atrophy ◽  
Cajal Body ◽  
Cajal Bodies ◽  
Proliferating Cells ◽  
Sm Proteins ◽  
Coiled Bodies

The spliceosomal snRNAs U1, U2, U4, and U5 are synthesized in the nucleus, exported to the cytoplasm to assemble with Sm proteins, and reimported to the nucleus as ribonucleoprotein particles. Recently, two novel proteins involved in biogenesis of small nuclear ribonucleoproteins (snRNPs) were identified, the Spinal muscular atrophy disease gene product (SMN) and its associated protein SIP1. It was previously reported that in HeLa cells, SMN and SIP1 form discrete foci located next to Cajal (coiled) bodies, the so-called “gemini of coiled bodies” or “gems.” An intriguing feature of gems is that they do not appear to contain snRNPs. Here we show that gems are present in a variable but small proportion of rapidly proliferating cells in culture. In the vast majority of cultured cells and in all primary neurons analyzed, SMN and SIP1 colocalize precisely with snRNPs in the Cajal body. The presence of SMN and SIP1 in Cajal bodies is confirmed by immunoelectron microscopy and by microinjection of antibodies that interfere with the integrity of the structure. The association of SMN with snRNPs and coilin persists during cell division, but at the end of mitosis there is a lag period between assembly of new Cajal bodies in the nucleus and detection of SMN in these structures, suggesting that SMN is targeted to preformed Cajal bodies. Finally, treatment of cells with leptomycin B (a drug that blocks export of U snRNAs to the cytoplasm and consequently import of new snRNPs into the nucleus) is shown to deplete snRNPs (but not SMN or SIP1) from the Cajal body. This suggests that snRNPs flow through the Cajal body during their biogenesis pathway.

The spinal muscular atrophy gene product regulates neurite outgrowth: importance of the C terminus

2007 ◽  
Vol 21 (7) ◽  
pp. 1492-1502 ◽  
Author(s):  
Jeroen Bergeijk ◽  
Katharina Rydel‐Könecke ◽  
Claudia Grothe ◽  
Peter Claus
Keyword(s):  
Spinal Muscular Atrophy ◽  
Neurite Outgrowth ◽  
Gene Product ◽  
Muscular Atrophy ◽  
C Terminus

scholarly journals Osteoclast-stimulating Factor Interacts with the Spinal Muscular Atrophy Gene Product to Stimulate Osteoclast Formation

2001 ◽  
Vol 276 (44) ◽  
pp. 41035-41039 ◽  
Author(s):  
Noriyoshi Kurihara ◽  
Cheikh Menaa ◽  
Hidefumi Maeda ◽  
David J. Haile ◽  
Sakamuri V. Reddy
Keyword(s):  
Spinal Muscular Atrophy ◽  
Gene Product ◽  
Muscular Atrophy ◽  
Osteoclast Formation ◽  
Stimulating Factor
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