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found that SMARCAL1 was transcriptionally inhibited by E2F6, an important cell cycle regulator. Over-expression of E2F6 in zebrafish embryos reduced the expression of smarcal1 mRNA and induced developmental defects similar to those in smarcal1 morphants
The main roles of SMARCAL1 in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress are reviewed.
our data reveal the critical function of the DNA replication stress response and, specifically, Smarcal1 in hematopoietic cell survival and tumor development. Our results also provide important insight into the immunodeficiency observed in individuals with mutations in SMARCAL1 by suggesting that it is an HSPC defect.
results provide the first identification, to our knowledge, of an endogenous source of replication stress that requires SMARCAL1 for resolution and define differences between members of this class of replication fork-repair enzymes.
the role of SMARCAL1 in the pathogenesis of Schimke immuno-osseous dysplasia
Mutation of predicted DNA-binding residues in the HARP domain dramatically reduced fork binding and regression activities of SMARCAL1 catalytic domain.
did not find evidence of defective NER or NHEJ; however, Smarcal1-deficient mice were hypersensitive to several genotoxic agents
SMARCAL1 annealing helicase buffers fluctuations in gene expression and that alterations in gene expression contribute to the penetrance of SIOD.
Downregulation of SMARCAL1 and BRG1 results in downregulation of ATM and ATR and therefore, mitotic abnormalities.
Mcm10 is a potent DNA strand-annealing protein that inhibits fork regression by SMARCAL1.
A large number of SNF2 family, DNA and ATP-dependent motor proteins are needed during transcription, DNA replication, and DNA repair to manipulate protein-DNA interactions and change DNA structure. SMARCAL1, ZRANB3, and HLTF are three related members of this family with specialized functions that maintain genome stability during DNA replication. [review]
BRG1 and SMARCAL1, members of the ATP-dependent chromatin remodelling family, are shown to co-regulate the transcription of DROSHA, DGCR8, and DICER in response to double-strand DNA breaks.
depletion of SMARCAL1, a SNF2-family DNA translocase that remodels stalled forks, restores replication fork stability and reduces the formation of replication stress-induced DNA breaks and chromosomal aberrations in BRCA1/2-deficient cells. In addition to SMARCAL1, other SNF2-family fork remodelers, including ZRANB3 and HLTF, cause nascent DNA degradation and genomic instability
the mechanism of SMARCAL1 function in maintaining genome stability
deficiency of a SMARCAL1 ortholog altering the chromatin structure of a gene
Results provide evidence that BRG1 and SMARCAL1 regulate each other. BRG1 binds to the SMARCAL1 promoter, while SMARCAL1 binds to the brg1 promoter. During DNA damage, the occupancy of SMARCAL1 on the brg1 promoter increases coinciding with an increase in BRG1 occupancy on the SMARCAL1 promoter, leading to increased brg1 and SMARCAL1 transcripts respectively.
the replication stress response protein SMARCAL1 is a critical regulator of alternative lengthening of telomeres activity.
SMARCAL1 negatively regulates c-myc transcription by altering the conformation of its promoter region during differentiation.
Mutations in human SMARCAL1 that result in loss in ATPase activity lead to increased replication stress and therefore possibly manifestation of Schimke immuno-osseous dysplasia.
The results suggest that Smarcal1 enhances nonhomologous end-joining repair, presumably by interacting with RPA at unwound single-strand sequences and then facilitating annealing at double-strand-break ends.
In addition to its annealing helicase activity, which eliminates the natural binding substrate for RPA, HARP blocks the phosphorylation of RPA by DNA-PK.
We present here the first evidence of intrinsic chromosomal instability in a severe SMARCAL1-deficient patient with a clinical picture of SIOD.
Conserved motifs are required for RPA32 binding the the N-terminus of SMARCAL1.
report provided the clinical and genetic description of a mild phenotype of Schimke immuno-osseous dysplasia associated with nephrotic proteinuria, decreasing after combined therapy with ACE inhibitors and sartans.
Brca2 and Rad51 prevent formation of abnormal DNA replication intermediates, whose processing by Smarcal1 and Mre11 predisposes to genome instability.
The protein encoded by this gene is a member of the SWI/SNF family of proteins. Members of this family have helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The encoded protein shows sequence similarity to the E. coli RNA polymerase-binding protein HepA. Mutations in this gene are a cause of Schimke immunoosseous dysplasia (SIOD), an autosomal recessive disorder with the diagnostic features of spondyloepiphyseal dysplasia, renal dysfunction, and T-cell immunodeficiency.
SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a-like 1
, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin a-like 1
, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
, hepA-related protein
, sucrose nonfermenting protein 2-like 1
, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1-like
, ATP-driven annealing helicase
, HepA-related protein
, SMARCA-like protein 1
, Sucrose nonfermenting protein 2-like 1