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1.
Med Sci Educ ; 34(1): 193-200, 2024 Feb.
Article in English | MEDLINE | ID: mdl-38510385

ABSTRACT

Considering laboratory results are used to make medical decisions, a fundamental understanding of laboratory medicine is paramount to enhance patient care, optimize health care cost containment, and prevent legal repercussions. With increasing laboratory testing complexity, this education is needed now more than ever. This article is a call to action to have medical schools adequately incorporate practical laboratory medicine content into their undergraduate medical education (UME) curricula. The authors discuss the definition of laboratory medicine, what it encompasses, who uses it and why it matters, and propose that a core laboratory medicine curriculum is a necessary part of UME.

2.
Curr Biol ; 11(14): 1079-88, 2001 Jul 24.
Article in English | MEDLINE | ID: mdl-11509230

ABSTRACT

BACKGROUND: The survival of motor neurons (SMN) protein is the protein product of the spinal muscular atrophy (SMA) disease gene. SMN and its associated proteins Gemin2, Gemin3, and Gemin4 form a large complex that plays a role in snRNP assembly, pre-mRNA splicing, and transcription. The functions of SMN in these processes are mediated by a direct interaction of SMN with components of these machineries, such as Sm proteins and RNA helicase A. RESULTS: We show that SMN binds directly to fibrillarin and GAR1. Fibrillarin and GAR1 are specific markers of the two classes of small nucleolar ribonucleoprotein particles (snoRNPs) that are involved in posttranscriptional processing and modification of ribosomal RNA. SMN interaction requires the arginine- and glycine-rich domains of both fibrillarin and GAR1 and is defective in SMN mutants found in some SMA patients. Coimmunoprecipitations demonstrate that the SMN complex associates with fibrillarin and with GAR1 in vivo. The inhibition of RNA polymerase I transcription causes a transient redistribution of SMN to the nucleolar periphery and loss of fibrillarin and GAR1 colocalization with SMN in gems. Furthermore, the expression of a dominant-negative mutant of SMN (SMNDeltaN27) causes snoRNPs to accumulate outside of the nucleolus in structures that also contain components of gems and coiled (Cajal) bodies. CONCLUSIONS: These findings identify fibrillarin and GAR1 as novel interactors of SMN and suggest a function for the SMN complex in the assembly and metabolism of snoRNPs. We propose that the SMN complex performs functions necessary for the biogenesis and function of diverse ribonucleoprotein complexes.


Subject(s)
Chromosomal Proteins, Non-Histone/metabolism , Nerve Tissue Proteins/metabolism , Ribonucleoproteins, Small Nucleolar/metabolism , Arginine/chemistry , Binding Sites , Cell Nucleolus/metabolism , Conserved Sequence , Cyclic AMP Response Element-Binding Protein , Glycine/chemistry , HeLa Cells , Humans , Mutation , Nerve Tissue Proteins/chemistry , Nerve Tissue Proteins/genetics , Protein Binding , Protein Structure, Tertiary , RNA-Binding Proteins , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , SMN Complex Proteins , Transcription, Genetic
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