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A homozygous frameshift mutation in ARPC1B (p.Val91Trpfs*30) was identified in a child with microthrombocytopenia, eosinophilia and inflammatory disease. Platelet lysates contained no ARPC1B protein and reduced Arp2 (show ACTR2 Proteins)/3 complex. Missense ARPC1B mutations were identified in an unrelated patient with similar symptoms and ARPC1B deficiency. ARPC1B-deficient platelets are microthrombocytes with abnormal spreading behavior.
The binding and catalytic behavior of purified AID was tested on DNA/RNA hybrid substrates bearing either random sequences or GC-rich (show RELB Proteins) sequences simulating Ig S regions. AID exhibited a higher affinity for binding DNA/RNA hybrid substrates made of S region sequences, than any other DNA substrates. In the absence of any other cellular processes or factors, AID itself favors binding and mutating S-region DNA/RNA hybrids.
A homozygous 2 bp deletion, n.c.G623DEL-TC (p.V208VfsX20), in Arp2 (show ACTR2 Proteins)/3 complex component ARPC1B that causes a frame shift resulting in premature termination was found in 2 brothers with hematopoietic and immunologic symptoms reminiscent of Wiskott-Aldrich syndrome. Wild-type ARPC1B but not mutant was able to rescue a deficiency in a zebrafish model. ARPC1B expression is restricted to hematopoietic cells.
This study identified two low-frequency nonsynonymous variants at FKBPL (show FKBPL Proteins) (rs200847762, OR = 0.34, 95% CI = 0.20-0.57, P = 4.31 x 10-5) and ARPC1B (rs1045012, OR = 0.56, 95% CI = 0.43-0.74, P = 4.30 x 10-5) associated with breast cancer risk.
silencing of AID in human bone marrow cells skews differentiation toward myelomonocytic lineage. However, in contrast to Tet2 loss, Aid loss does not contribute to enhanced HSC (show FUT1 Proteins) self-renewal or cooperate with Flt3 (show FLT3 Proteins)-ITD to induce myeloid transformation. Genome-wide transcription and differential methylation analysis uncover the critical role of Aid as a key epigenetic regulator
These findings indicated that TNF-alpha (show TNF Proteins)-induced AID expression is involved with class switch recombination in cancer.
Finnish founder allele causing HIGM2 (show AICDA Proteins) identified.
low-expression of ARPC1B is significantly associated with LNM and advanced tumor staging whereas high expression of Cav-1 (show CAV1 Proteins) can be a prognostic indicator for poor prognosis in OSCC patients.
this study reports a case of growth hormone (show GH1 Proteins) deficiency with an autosomal recessive Hyper-immunoglobulin M syndrome by phenotype and genotype, with a novel mutation in AICDA (show AICDA Proteins) that has not been reported formerly
AICDA (show AICDA Proteins)/APOBEC family of cytidine deaminases is significant in innate immunity, as it restricts numerous viruses, including HBV, through hypermutationdependent and independent mechanisms. (Review)
crystal structure of Arp2 (show ACTR2 Proteins)/3 complex
These results demonstrate an important role for CRMP-1 (show CRMP1 Proteins) in Listeria actin comet tail formation and open the possibility that CRMP-1 (show CRMP1 Proteins) controls cell motility by modulating Arp2 (show ACTR2 Proteins)/3 activation.
The GMF-Arp2 interface reveals how the ADF-H actin-binding domain in GMF is exploited to specifically recognize Arp2/3 complex and not actin.
interacts with contactin and N-WASp
Data show that L. monocytogenes motility can be separated into an Arp2 (show ACTR2 Proteins)/3-dependent nucleation phase, and an Arp2 (show ACTR2 Proteins)/3-independent elongation phase which is dependent upon fascin (show FSCN1 Proteins).
crystal structures of Arp2/3 complex with bound ATP or ADP
WASp stabilizes p35-dependent closure of the complex, holding Arp2 and Arp3 closer together to nucleate an actin filament.
domain rearrangements of Arp2 and Arp3 result in a closed conformational state consistent with an "actin-dimer" model for the active state
This gene encodes one of seven subunits of the human Arp2/3 protein complex. This subunit is a member of the SOP2 family of proteins and is most similar to the protein encoded by gene ARPC1A. The similarity between these two proteins suggests that they both may function as p41 subunit of the human Arp2/3 complex that has been implicated in the control of actin polymerization in cells. It is possible that the p41 subunit is involved in assembling and maintaining the structure of the Arp2/3 complex. Multiple versions of the p41 subunit may adapt the functions of the complex to different cell types or developmental stages. This protein also has a role in centrosomal homeostasis by being an activator and substrate of the Aurora A kinase.
ARP2/3 protein complex subunit p41
, actin-related protein 2/3 complex subunit 1B
, arp2/3 complex 41 kDa subunit
, Actin-related protein complex 1b
, actin related protein 2/3 complex subunit 1B
, ARP2/3 complex 41 kDa subunit
, actin related protein 2/3 complex, subunit 1A, 41kDa
, actin related protein 2/3 complex, subunit 1B, 41kDa
, actin-related protein 2/3 complex subunit 1B-like