Ignet

Gene Information

Gene symbol: CFL1

Gene name: cofilin 1 (non-muscle)

HGNC ID: 1874

Related Genes

#	Gene Symbol	Number of hits
1	CORO2B	1 hits
2	LGMN	1 hits
3	LIMK1	1 hits
4	NPHS1	1 hits
5	NPHS2	1 hits
6	PDLIM5	1 hits
7	PTEN	1 hits
8	SYNPO	1 hits
9	TESK1	1 hits
10	TNC	1 hits
11	VCAM1	1 hits
12	VCL	1 hits
13	VIM	1 hits

Related Sentences

#	PMID	Sentence
1	20472933	Because podocyte intercellular junction receptor Nephrin plays a role in regulating actin dynamics, and given the described role of cofilin in actin filament polymerization and severing, we hypothesized that cofilin-1 activity is regulated by Nephrin and is necessary in normal podocyte actin dynamics.
2	20472933	Nephrin activation induced cofilin dephosphorylation via intermediaries that include phosphatidylinositol 3-kinase, SSH1, 14-3-3, and LIMK in a cell culture model.
3	20472933	This Nephrin-induced cofilin activation required a direct interaction between Nephrin and the p85 subunit of phosphatidylinositol 3-kinase.
4	21336536	In elegant biochemical studies, Garg et al. established that cofilin-1 activity is regulated by nephrin, which is part of the slit diaphragm complex.
5	24737737	However, whether synaptopodin is the only target of CsA or whether the antiproteinuric role of CsA is played by regulating cofilin-1 in podocytes has not been studied.
6	24737737	In the present study, changes in the expression and distribution of nephrin, synaptopodin, cofilin-1 and phosphorylated cofilin-1 (pho-cofilin-1) were detected in both puromycin aminonucleoside (PAN) induced nephrotic rats treated with CsA and cultured podocytes exposed to PAN with/without CsA.
7	24737737	Cofilin-1, synaptopodin mRNA was knocked down or combined by siRNA to investigate whether cofilin-1 was critical for the protective effect of CsA and whether the effect of CsA on cofilin-1 was independent of its effect on synaptopodin.
8	24737737	We found that CsA reduced proteinuria and repaired FP effacement of PAN-induced nephropathy, restored expression of nephrin, synaptopodin, cofilin-1, pho-cofilin-1 both in vivo and in vitro.
9	24737737	Synaptopodin knocked down had no effect on cofilin-1.
10	24737737	The protective effect of CsA decreased significantly when cofilin-1 and synaptopodin were simultaneously knocked down compared to only cofilin-1 knock down.
11	24737737	However, whether synaptopodin is the only target of CsA or whether the antiproteinuric role of CsA is played by regulating cofilin-1 in podocytes has not been studied.
12	24737737	In the present study, changes in the expression and distribution of nephrin, synaptopodin, cofilin-1 and phosphorylated cofilin-1 (pho-cofilin-1) were detected in both puromycin aminonucleoside (PAN) induced nephrotic rats treated with CsA and cultured podocytes exposed to PAN with/without CsA.
13	24737737	Cofilin-1, synaptopodin mRNA was knocked down or combined by siRNA to investigate whether cofilin-1 was critical for the protective effect of CsA and whether the effect of CsA on cofilin-1 was independent of its effect on synaptopodin.
14	24737737	We found that CsA reduced proteinuria and repaired FP effacement of PAN-induced nephropathy, restored expression of nephrin, synaptopodin, cofilin-1, pho-cofilin-1 both in vivo and in vitro.
15	24737737	Synaptopodin knocked down had no effect on cofilin-1.
16	24737737	The protective effect of CsA decreased significantly when cofilin-1 and synaptopodin were simultaneously knocked down compared to only cofilin-1 knock down.
17	24737737	However, whether synaptopodin is the only target of CsA or whether the antiproteinuric role of CsA is played by regulating cofilin-1 in podocytes has not been studied.
18	24737737	In the present study, changes in the expression and distribution of nephrin, synaptopodin, cofilin-1 and phosphorylated cofilin-1 (pho-cofilin-1) were detected in both puromycin aminonucleoside (PAN) induced nephrotic rats treated with CsA and cultured podocytes exposed to PAN with/without CsA.
19	24737737	Cofilin-1, synaptopodin mRNA was knocked down or combined by siRNA to investigate whether cofilin-1 was critical for the protective effect of CsA and whether the effect of CsA on cofilin-1 was independent of its effect on synaptopodin.
20	24737737	We found that CsA reduced proteinuria and repaired FP effacement of PAN-induced nephropathy, restored expression of nephrin, synaptopodin, cofilin-1, pho-cofilin-1 both in vivo and in vitro.
21	24737737	Synaptopodin knocked down had no effect on cofilin-1.
22	24737737	The protective effect of CsA decreased significantly when cofilin-1 and synaptopodin were simultaneously knocked down compared to only cofilin-1 knock down.
23	24737737	However, whether synaptopodin is the only target of CsA or whether the antiproteinuric role of CsA is played by regulating cofilin-1 in podocytes has not been studied.
24	24737737	In the present study, changes in the expression and distribution of nephrin, synaptopodin, cofilin-1 and phosphorylated cofilin-1 (pho-cofilin-1) were detected in both puromycin aminonucleoside (PAN) induced nephrotic rats treated with CsA and cultured podocytes exposed to PAN with/without CsA.
25	24737737	Cofilin-1, synaptopodin mRNA was knocked down or combined by siRNA to investigate whether cofilin-1 was critical for the protective effect of CsA and whether the effect of CsA on cofilin-1 was independent of its effect on synaptopodin.
26	24737737	We found that CsA reduced proteinuria and repaired FP effacement of PAN-induced nephropathy, restored expression of nephrin, synaptopodin, cofilin-1, pho-cofilin-1 both in vivo and in vitro.
27	24737737	Synaptopodin knocked down had no effect on cofilin-1.
28	24737737	The protective effect of CsA decreased significantly when cofilin-1 and synaptopodin were simultaneously knocked down compared to only cofilin-1 knock down.
29	24737737	However, whether synaptopodin is the only target of CsA or whether the antiproteinuric role of CsA is played by regulating cofilin-1 in podocytes has not been studied.
30	24737737	In the present study, changes in the expression and distribution of nephrin, synaptopodin, cofilin-1 and phosphorylated cofilin-1 (pho-cofilin-1) were detected in both puromycin aminonucleoside (PAN) induced nephrotic rats treated with CsA and cultured podocytes exposed to PAN with/without CsA.
31	24737737	Cofilin-1, synaptopodin mRNA was knocked down or combined by siRNA to investigate whether cofilin-1 was critical for the protective effect of CsA and whether the effect of CsA on cofilin-1 was independent of its effect on synaptopodin.
32	24737737	We found that CsA reduced proteinuria and repaired FP effacement of PAN-induced nephropathy, restored expression of nephrin, synaptopodin, cofilin-1, pho-cofilin-1 both in vivo and in vitro.
33	24737737	Synaptopodin knocked down had no effect on cofilin-1.
34	24737737	The protective effect of CsA decreased significantly when cofilin-1 and synaptopodin were simultaneously knocked down compared to only cofilin-1 knock down.
35	24737737	However, whether synaptopodin is the only target of CsA or whether the antiproteinuric role of CsA is played by regulating cofilin-1 in podocytes has not been studied.
36	24737737	In the present study, changes in the expression and distribution of nephrin, synaptopodin, cofilin-1 and phosphorylated cofilin-1 (pho-cofilin-1) were detected in both puromycin aminonucleoside (PAN) induced nephrotic rats treated with CsA and cultured podocytes exposed to PAN with/without CsA.
37	24737737	Cofilin-1, synaptopodin mRNA was knocked down or combined by siRNA to investigate whether cofilin-1 was critical for the protective effect of CsA and whether the effect of CsA on cofilin-1 was independent of its effect on synaptopodin.
38	24737737	We found that CsA reduced proteinuria and repaired FP effacement of PAN-induced nephropathy, restored expression of nephrin, synaptopodin, cofilin-1, pho-cofilin-1 both in vivo and in vitro.
39	24737737	Synaptopodin knocked down had no effect on cofilin-1.
40	24737737	The protective effect of CsA decreased significantly when cofilin-1 and synaptopodin were simultaneously knocked down compared to only cofilin-1 knock down.
41	29162887	Using quantitative focal adhesome proteomics we identify the recruitment of CFL1 via CORO2B to focal adhesions as an underlying mechanism.
42	30115939	ROK activates LIM kinases (LIMKs), which phosphorylate and inhibit the actin depolymerizing factor cofilin 1 (CFL1).
43	30115939	CFL1 is also phosphorylated by testis-specific kinase 1 (TESK1) on the same serine residue.
44	30115939	ROK activates LIM kinases (LIMKs), which phosphorylate and inhibit the actin depolymerizing factor cofilin 1 (CFL1).
45	30115939	CFL1 is also phosphorylated by testis-specific kinase 1 (TESK1) on the same serine residue.
46	31813249	PTEN directly dephosphorylates and activates the actin-depolymerizing factor cofilin-1, leading to depolymerization of filamentous actin (F-actin), which is necessary for endocytosis.
47	31813249	Notably, inhibition of PTEN resulted in the phosphorylation and inactivation of cofilin-1, leading to F-actin formation that enhanced the endocytosis of lipoproteins in podocytes.
48	31813249	PTEN directly dephosphorylates and activates the actin-depolymerizing factor cofilin-1, leading to depolymerization of filamentous actin (F-actin), which is necessary for endocytosis.
49	31813249	Notably, inhibition of PTEN resulted in the phosphorylation and inactivation of cofilin-1, leading to F-actin formation that enhanced the endocytosis of lipoproteins in podocytes.
50	33024228	Western blot and immunocytochemistry confirmed the alteration in the protein expression of tubulin, vimentin, podocin, cofilin-1, vinculin, E-cadherin, nephrin, VCAM-1, tenascin-C, and β-catenin.
51	35217650	Asparaginyl endopeptidase protects against podocyte injury in diabetic nephropathy through cleaving cofilin-1.
52	35217650	Mechanistically, we found that AEP directly cleaved the actin-binding protein cofilin-1 after the asparagine 138 (N138) site.
53	35217650	The protein levels of endogenous cofilin-1 1-138 fragments were upregulated in diabetic podocytes, consistent with the changes in AEP levels.
54	35217650	Taken together, our data suggest a protective role of elevated AEP in podocyte injury during DN progression through cleaving cofilin-1 to maintain podocyte cytoskeleton dynamics and defend damage.
55	35217650	Asparaginyl endopeptidase protects against podocyte injury in diabetic nephropathy through cleaving cofilin-1.
56	35217650	Mechanistically, we found that AEP directly cleaved the actin-binding protein cofilin-1 after the asparagine 138 (N138) site.
57	35217650	The protein levels of endogenous cofilin-1 1-138 fragments were upregulated in diabetic podocytes, consistent with the changes in AEP levels.
58	35217650	Taken together, our data suggest a protective role of elevated AEP in podocyte injury during DN progression through cleaving cofilin-1 to maintain podocyte cytoskeleton dynamics and defend damage.
59	35217650	Asparaginyl endopeptidase protects against podocyte injury in diabetic nephropathy through cleaving cofilin-1.
60	35217650	Mechanistically, we found that AEP directly cleaved the actin-binding protein cofilin-1 after the asparagine 138 (N138) site.
61	35217650	The protein levels of endogenous cofilin-1 1-138 fragments were upregulated in diabetic podocytes, consistent with the changes in AEP levels.
62	35217650	Taken together, our data suggest a protective role of elevated AEP in podocyte injury during DN progression through cleaving cofilin-1 to maintain podocyte cytoskeleton dynamics and defend damage.
63	35217650	Asparaginyl endopeptidase protects against podocyte injury in diabetic nephropathy through cleaving cofilin-1.
64	35217650	Mechanistically, we found that AEP directly cleaved the actin-binding protein cofilin-1 after the asparagine 138 (N138) site.
65	35217650	The protein levels of endogenous cofilin-1 1-138 fragments were upregulated in diabetic podocytes, consistent with the changes in AEP levels.
66	35217650	Taken together, our data suggest a protective role of elevated AEP in podocyte injury during DN progression through cleaving cofilin-1 to maintain podocyte cytoskeleton dynamics and defend damage.