IndraLab

Statements


ACVR2A affects ACVR1B
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3 | 1 7

sparser
"The type II receptor ActRIIA and the type I receptor Alk4, which form heteromeric complexes in NMuMG cells ( xref ), were detected in cell lysates with higher levels of the type II receptor observed in E1KD cells."

No evidence text available

sparser
"Compound NUCC-555 blocked activin/ ActRIIA complex binding with ALK4 in the Blitz label-free binding assay, further supporting our view that the functional effects measured in our cellular assays are caused by NUCC-555 preventing the activin/ActRIIA complex from binding ALK4."

sparser
"Our results show that ACVR2A can form stable heteromeric complexes with ALK4 (an activin type I receptor), as well as with several BMP type I receptors (ALK2/3/6)."

reach
"70 NUCC-555 strongly inhibited activin and ActRIIA complex binding to ALK4 at 25 microM, whereas there was no inhibition of myostatin / ActRIIA complex binding to ALK4 at the same drug concentration in the Blitz binding system equipped with the " dip and read " probe sensor."

No evidence text available

No evidence text available

sparser
"Two subunits of Inhba form the homodimer Activin A, which signals through canonical ALK4-ACVR2 receptor complexes activating the transcription factors SMAD2 and SMAD3."
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sparser
"The precise mechanism of this antagonism is not yet clear, but preliminary data suggest that in the presence of InhBP and inhibin B, there is an abrogation of actRII's association with ALK4 in respons[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"These data expand our understanding of how endocrine inhibin achieves potent antagonism of local, constitutive activin action in the pituitary, through a combined mechanism of competitive binding of both ActRII and ALK4 by each subunit of the inhibin heterodimer, in conjunction with the co-receptor betaglycan, to block activin receptor-ligand binding, complex assembly, and downstream signaling."
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sparser
"Follistatin acts by masking the activin regions crucial for the interaction with ActRII and ALK4. xref "

reach
"Also in the Activin : ActRII complex no direct contact between the two receptor ECDs was observed with the closest proximity being 31A, however, whether or not receptor interaction between ActRII and ActRIIB and ALK4 occur, awaits structural data with the ALK4 extracellular domain."

reach
"In contrast to TGFbeta, TRAF6 recruitment to the ALK4 and ActRII complex was significantly decreased early after infection although it was restored at 18 hpi (XREF_FIG)."

reach
"ActRII binds to activin in combination with ALK4, but also binds both BMP2 and BMP7 in the presence of BMP type I receptors (Carcamo et al., 1994; Yamashita et al., 1995; Willis et al., 1996)."

reach
"ALK4 and ActRII interactions increased within 30 ' post infection and then decreased by 2 hpi (XREF_FIG and XREF_SUPPLEMENTARY)."

reach
"The phosphorylation as a consequence of the interaction between ActR-IB and ActR-II allows ActR-IB to spread the signal transduction, which is the same as mechanism of activation of the TGF-receptor ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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sparser
"Provided that activin B elicits BR-mediated signaling via ALK2 and ActRIIA and AR-mediated signaling via ALK4 and ActRIIs, we hypothesized that ALK2 forms complex with ALK4 as well as ActRII."

sparser
"These results suggest that ALK2 intrinsically associate with ALK4 or ActRIIA or both; especially the band at ~360 kDa (band 1), which was the band with common size detected in Western blot using antibody against Flag, HA or Myc, may indicate receptor complex of ALK2-ALK4-ActRIIA."

sparser
"As mentioned previously, Activin A functions through binding to the ActRII-ALK4 or ActRII-ALK2 receptor complex to initiate Smad-dependent or independent signaling cascades."

No evidence text available

sparser
"Activin A interacts with the type II activin receptors, ActRIIA and ActRIIB, leading to the recruitment and activation of the type I receptor Alk4 and subsequent phosphorylation of Smad2/3."

sparser
"Activins bind to activin receptor type IIA (ActRIIA) or ActRIIB in a complex with ALK4, while BMPs signal via BMP type II receptor (BMPRII), ActRIIA or ActRIIB, in combination with ALK1, 2, 3 or 6."
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sparser
"GDF3 was reported to be involved in both canonical pathways triggered by TGFB family members: (1) extracellular inhibition of BMPs xref and (2) induction of SMAD2/3 phosphorylation due to binding to Activin A receptors type IB or IC (ACVRIB, ACVRIC) and Activin A receptors type IIA or IIB (ACVRIIA, ACVRIIB) in cooperation with obligatory co-receptor teratocarcinoma-derived growth factor 1 (TDGF1) xref , xref ."
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sparser
"The interactions of ISM1 with NODAL, ACVR1B, and ACVR2A raise the possibility that ISM1 may disturb NODAL signaling through interfering with the interaction between NODAL ligand and receptor complex."

sparser
"Together, these results indicate that activin and Nodal assemble structurally and functionally similar signaling complexes containing ActRII, ALK4 and Cripto."
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sparser
"Activin A primarily binds to the type 1 receptors ALK4 or ALK7 in complex with ACVR2A or ACVR2B, causing activation of SMAD2 or SMAD3 [ xref ]."
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sparser
"ACVR2A forms an activin receptor complex with ACVR1B ."
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sparser
"In support of this, covalent crosslinking experiments demonstrated that activin-A assembles complexes containing Cripto, ActRII and ALK4 when these proteins were overexpressed in 293T cells or when they were expressed at endogenous levels in P19 cells [ xref ]."
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sparser
"1 and 2 ), a quaternary complex of ActRIIA, ActRIB, Smad 3 and ARIP1 can form."
ACVR1B affects ACVR1C, ACVR2A, GDF11, GTF2B, and TGFBR1
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sparser
"As one member of the TGF‐β superfamily, GDF11 binds to activin type IIA (ActRIIA) or type IIB (ActRIIB) and type I activin receptor‐like kinase (ALK) receptors ALK4, ALK5, and ALK7 to elicit signal transduction via SMAD2/3 (Andersson et al., xref ; Oh et al., xref ; Walker et al., xref )."
ACVR1B affects ACVR1C, ACVR2A, and ACVR2B
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sparser
"Activin A primarily binds to the type 1 receptors ALK4 or ALK7 in complex with ACVR2A or ACVR2B, causing activation of SMAD2 or SMAD3 [ xref ]."