Abstract
Scapuloperoneal (SP) syndrome encompasses heterogeneous neuromuscular disorders characterized by weakness in the shoulder-girdle and peroneal muscles. In a large Italian-American pedigree with dominant SP myopathy (SPM) previously linked to chromosome 12q, we have mapped the disease to Xq26, and, in all of the affected individuals, we identified a missense change (c.365G-->C) in the FHL1 gene encoding four-and-a-half-LIM protein 1 (FHL1). The mutation substitutes a serine for a conserved trypophan at amino acid 122 in the second LIM domain of the protein. Western blot analyses of muscle extracts revealed FHL1 loss that paralleled disease severity. FHL1 and an isoform, FHL1C, are highly expressed in skeletal muscle and may contribute to stability of sarcomeres and sarcolemma, myofibrillary assembly, and transcriptional regulation. This is the first report, to our knowledge, of X-linked dominant SP myopathy and the first human mutation in FHL1.
MeSH Terms
Amino Acid Sequence
Amino Acid Substitution
Female
Genes, Dominant
Genes, X-Linked
Humans
Intracellular Signaling Peptides and Proteins/chemistry,genetics
LIM Domain Proteins
Male
Models, Molecular
Molecular Sequence Data
Muscle Proteins/chemistry,genetics
Muscular Dystrophy, Emery-Dreifuss/genetics
Mutation, Missense
Pedigree
Protein Structure, Tertiary
Chemicals
FHL1 protein, human
Intracellular Signaling Peptides and Proteins
LIM Domain Proteins
Muscle Proteins
Authors & Affiliations
16 authors, click to expand affiliations / ORCID
Quinzii Catarina M
Department of Neurology, Columbia University Medical Center, New York, NY 10032, USA.
Vu Tuan H
Min K Christopher
Tanji Kurenai
Barral Sandra
Grewal Raji P
Kattah Andrea
Camaño Pilir
Otaegui David
Kunimatsu Teruhito
Blake David M
Wilhelmsen Kirk C
Rowland Lewis P
Hays Arthur P
Bonilla Eduardo
Hirano Michio
References (24)
24 references, click to expand
-
The LIM proteins FHL1 and FHL3 are expressed differently in skeletal muscle.
Biochem Biophys Res Commun. 1999 Feb 16;255(2):245-50
PMID: 10049693
-
Chromosomal mapping, tissue distribution and cDNA sequence of four-and-a-half LIM domain protein 1 (FHL1).
Gene. 1998 Aug 17;216(1):163-70
PMID: 9714789
-
Characterization of two isoforms of the skeletal muscle LIM protein 1, SLIM1. Localization of SLIM1 at focal adhesions and the isoform slimmer in the nucleus of myoblasts and cytoplasm of myotubes suggests distinct roles in the cytoskeleton and in nuclear-cytoplasmic communication.
J Biol Chem. 1999 Sep 17;274(38):27083-91
PMID: 10480922
-
Characterization of a brain-specific nuclear LIM domain protein (FHL1B) which is an alternatively spliced variant of FHL1.
Gene. 1999 Sep 3;237(1):253-63
PMID: 10524257
-
The LIM domain: from the cytoskeleton to the nucleus.
Nat Rev Mol Cell Biol. 2004 Nov;5(11):920-31
PMID: 15520811
-
[On the nosological role of the scapulo-peroneal syndrome].
Dtsch Z Nervenheilkd. 1962;183:377-82
PMID: 13905444
-
The multifunctional roles of the four-and-a-half-LIM only protein FHL2.
Cell Mol Life Sci. 2006 Feb;63(3):268-84
PMID: 16389449
-
Four and a half LIM protein 1 binds myosin-binding protein C and regulates myosin filament formation and sarcomere assembly.
J Biol Chem. 2006 Mar 17;281(11):7666-83
PMID: 16407297
-
MYH7 gene mutation in myosin storage myopathy and scapulo-peroneal myopathy.
Neuromuscul Disord. 2007 Apr;17(4):321-9
PMID: 17336526
-
Scapuloperoneal syndrome type Kaeser and a wide phenotypic spectrum of adult-onset, dominant myopathies are associated with the desmin mutation R350P.
Brain. 2007 Jun;130(Pt 6):1485-96
PMID: 17439987
-
Characterization of tissue-specific LIM domain protein (FHL1C) which is an alternatively spliced isoform of a human LIM-only protein (FHL1).
J Cell Biochem. 2001 Apr 2-27;82(1):1-10
PMID: 11400158
-
Skeletal muscle LIM protein 1 regulates integrin-mediated myoblast adhesion, spreading, and migration.
Am J Physiol Cell Physiol. 2003 Mar;284(3):C681-95
PMID: 12397030
-
Skeletal muscle LIM protein 1 (SLIM1/FHL1) induces alpha 5 beta 1-integrin-dependent myocyte elongation.
Am J Physiol Cell Physiol. 2003 Dec;285(6):C1513-26
PMID: 12917103
-
Protein degradation and protection against misfolded or damaged proteins.
Nature. 2003 Dec 18;426(6968):895-9
PMID: 14685250
-
Scapuloperoneal muscular atrophy.
Brain. 1965 Jun;88(2):407-18
PMID: 5828910
-
[The dystrophic type of scapuloperoneal syndrome].
Cesk Neurol. 1973 May;36(3):147-50
PMID: 4704112
-
Novel cysteine-rich motif and homeodomain in the product of the Caenorhabditis elegans cell lineage gene lin-11.
Nature. 1990 Apr 26;344(6269):876-9
PMID: 1970421
-
Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons.
Proteins. 1991;11(4):281-96
PMID: 1758883
-
Disruption of the mouse RBP-J kappa gene results in early embryonic death.
Development. 1995 Oct;121(10):3291-301
PMID: 7588063
-
Chromosome 12-linked autosomal dominant scapuloperoneal muscular dystrophy.
Ann Neurol. 1996 Apr;39(4):507-20
PMID: 8619529
-
Slim defines a novel family of LIM-proteins expressed in skeletal muscle.
Biochem Biophys Res Commun. 1996 Aug 14;225(2):632-8
PMID: 8753811
-
Linkage of scapuloperoneal spinal muscular atrophy to chromosome 12q24.1-q24.31.
Hum Mol Genet. 1996 Sep;5(9):1377-82
PMID: 8872481
-
LIM protein KyoT2 negatively regulates transcription by association with the RBP-J DNA-binding protein.
Mol Cell Biol. 1998 Jan;18(1):644-54
PMID: 9418910
-
Genomic structure, tissue expression and chromosomal location of the LIM-only gene, SLIM1.
Gene. 1999 May 31;232(2):203-7
PMID: 10352231