PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25096578-8 2014 Cofilin-1-severing/depolymerization activity is negatively regulated by phosphorylation of serine 3. Serine 91-97 cofilin 1 Homo sapiens 0-9 25549357-3 2014 Cofilin is a small actin-binding protein able to bind both forms of actin, globular and filament, and is regulated by phosphorylation at Serine 3. Serine 137-143 cofilin 1 Homo sapiens 0-7 25549357-4 2014 Following phosphorylation at serine 3 cofilin is inactive, therefore cannot bind actin molecules and cytoskeleton remodeling is impaired. Serine 29-35 cofilin 1 Homo sapiens 38-45 25096578-10 2014 Finally, a cofilin mutant that mimics phosphorylated Ser-3 can partially rescue necrosis in response to G5. Serine 53-56 cofilin 1 Homo sapiens 11-18 23897816-4 2013 The interaction is also regulated by phosphorylation at Ser-3 of mammalian cofilin, which inhibits binding to actin. Serine 56-59 cofilin 1 Homo sapiens 75-82 23934191-4 2014 LIM domain kinases (LIMK1 and 2) are substrate for Cdc42/Rac-PAK and modulate actin dynamics by phosphorylating cofilin at serine-3. Serine 123-129 cofilin 1 Homo sapiens 112-119 24214978-4 2013 O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion. Serine 19-22 cofilin 1 Homo sapiens 30-37 24003227-4 2013 One key molecule of T cell activation is the actin-remodeling protein cofilin, which is dephosphorylated on serine 3 upon T cell costimulation and has an essential role in formation of mature immune synapses between T cells and antigen-presenting cells. Serine 108-114 cofilin 1 Homo sapiens 70-77 23951242-13 2013 Cofilin phosphorylation at Ser-3 may induce conformational changes on the protein-protein interacting surface of the cofilin oligomer, thereby preventing and/or disrupting cofilin oligomer formation. Serine 27-30 cofilin 1 Homo sapiens 0-7 23951242-13 2013 Cofilin phosphorylation at Ser-3 may induce conformational changes on the protein-protein interacting surface of the cofilin oligomer, thereby preventing and/or disrupting cofilin oligomer formation. Serine 27-30 cofilin 1 Homo sapiens 117-124 23951242-7 2013 Furthermore, we found that formation of the cofilin oligomer is regulated by Ser-3 cofilin phosphorylation. Serine 77-80 cofilin 1 Homo sapiens 44-51 23951242-13 2013 Cofilin phosphorylation at Ser-3 may induce conformational changes on the protein-protein interacting surface of the cofilin oligomer, thereby preventing and/or disrupting cofilin oligomer formation. Serine 27-30 cofilin 1 Homo sapiens 172-179 23951242-7 2013 Furthermore, we found that formation of the cofilin oligomer is regulated by Ser-3 cofilin phosphorylation. Serine 77-80 cofilin 1 Homo sapiens 83-90 23153585-2 2013 Cofilin/ADF are inactivated by phosphorylation at the serine residue at position 3 by LIM-kinases (LIMKs) and testicular protein kinases (TESKs) and are reactivated by dephosphorylation by the slingshot (SSH) family of protein phosphatases and chronophin. Serine 54-60 cofilin 1 Homo sapiens 0-11 22270398-2 2012 Cofilin is inactivated by phosphorylation on Ser-3 by LIM-kinase1 (LIMK1) and is activated when protein phosphatase Slingshot-1L (SSH1L) dephosphorylates this residue. Serine 45-48 cofilin 1 Homo sapiens 0-7 21474314-5 2011 Previous work demonstrates that cofilin"s severing activity is tightly regulated through multiple mechanisms, including regulation of cofilin serine phosphorylation by Rho GTPases. Serine 142-148 cofilin 1 Homo sapiens 32-39 22790341-4 2012 The activity of ADF/cofilin is reversibly regulated by phosphorylation and dephosphorylation at Ser-3, with the phosphorylated form (P-cofilin) being inactive. Serine 96-99 cofilin 1 Homo sapiens 20-27 21923909-7 2011 Expression of Nef induced phosphorylation of CFL1 at serine 3 and LIMK1 at threonine 508, inhibited retinoid-receptor mediated reporter activity, and the expression of a number of genes that contain retinoid receptor binding sites in their promoters. Serine 53-59 cofilin 1 Homo sapiens 45-49 21474314-5 2011 Previous work demonstrates that cofilin"s severing activity is tightly regulated through multiple mechanisms, including regulation of cofilin serine phosphorylation by Rho GTPases. Serine 142-148 cofilin 1 Homo sapiens 134-141 17130184-2 2007 Only unphosphorylated cofilin binds actin and severs or depolymerizes filamentous actin (F-actin), and the inactive form of cofilin is phosphorylated at Ser 3. Serine 153-156 cofilin 1 Homo sapiens 124-131 19862699-5 2009 (2) Blocking cofilin"s ability to bind to actin via serine phosphorylation. Serine 52-58 cofilin 1 Homo sapiens 13-20 17470807-7 2007 The model identifies key ionic and hydrophobic interactions at the binding interface, including hydrogen-bonding between His-87 of actin to Ser-89 of cofilin that may control the charge dependence of cofilin binding. Serine 140-143 cofilin 1 Homo sapiens 150-157 17470807-7 2007 The model identifies key ionic and hydrophobic interactions at the binding interface, including hydrogen-bonding between His-87 of actin to Ser-89 of cofilin that may control the charge dependence of cofilin binding. Serine 140-143 cofilin 1 Homo sapiens 200-207 19567672-3 2009 PKD-mediated phosphorylation of serines 937 and 978 regulates SSH1L subcellular localization by binding of 14-3-3 proteins and thus impacts the control of local cofilin activation and actin remodeling during cell migration. Serine 32-39 cofilin 1 Homo sapiens 161-168 18459146-6 2008 Restriction of these amino acids increases the amount of profilin, cofilin and phosphorylation of cofilin-Ser(3). Serine 106-109 cofilin 1 Homo sapiens 98-105 15671020-1 2005 Cofilin, an essential regulator of actin filament dynamics, is inactivated by phosphorylation at Ser-3 and reactivated by dephosphorylation. Serine 97-100 cofilin 1 Homo sapiens 0-7 15660133-1 2005 Slingshot (SSH) phosphatases and LIM kinases (LIMK) regulate actin dynamics via a reversible phosphorylation (inactivation) of serine 3 in actin-depolymerizing factor (ADF) and cofilin. Serine 127-133 cofilin 1 Homo sapiens 177-184 15580268-1 2005 Cofilin is a key regulator of actin cytoskeletal dynamics whose activity is controlled by phosphorylation of a single serine residue. Serine 118-124 cofilin 1 Homo sapiens 0-7 15591324-10 2005 Sequencing of several cofilin gel spots revealed phosphorylation of serine 3, a post-translational modification associated with decreased actin binding and cytoskeletal reorganization. Serine 68-74 cofilin 1 Homo sapiens 22-29 16083947-4 2005 In unstimulated human peripheral blood T lymphocytes (PB-T) cofilin exists in its inactive ser-3-phosphorylated form. Serine 91-94 cofilin 1 Homo sapiens 60-67 15199148-6 2004 Rather, reduced ROCKII expression and attenuated phosphorylation of ADF/cofilin on serine 3 occurred. Serine 83-89 cofilin 1 Homo sapiens 72-79 15300782-2 2004 In higher vertebrates, cells often express as many as three different ADF/cofilin genes and each of these proteins may be phosphorylated on serine 3, giving rise to up to six different species. Serine 140-146 cofilin 1 Homo sapiens 74-81 15159416-2 2004 Cofilin is inactivated by phosphorylation at Ser-3 and reactivated by cofilin-phosphatase Slingshot-1L (SSH1L). Serine 45-48 cofilin 1 Homo sapiens 0-7 12837278-6 2003 The cofilin phosphorylation occurred at the serine residue of position 3 (Ser-3). Serine 44-50 cofilin 1 Homo sapiens 4-11 14645219-2 2004 Cofilin is inactivated by phosphorylation at Ser-3 by LIM kinase and reactivated by dephosphorylation by cofilin-phosphatase Slingshot (SSH). Serine 45-48 cofilin 1 Homo sapiens 0-7 14645219-5 2004 Consistent with this, the level of Ser-3-phosphorylated cofilin is increased in PTEN (phosphatase and tensin homolog deleted in chromosome 10)-overexpressing cells and decreased in PTEN-deficient cells. Serine 35-38 cofilin 1 Homo sapiens 56-63 12807904-4 2003 Cofilin is inactivated by phosphorylation on Ser-3 by LIM-kinase-1 (LIMK1) and is reactivated by a protein phosphatase Slingshot-1 (SSH1). Serine 45-48 cofilin 1 Homo sapiens 0-7 12837278-6 2003 The cofilin phosphorylation occurred at the serine residue of position 3 (Ser-3). Serine 74-77 cofilin 1 Homo sapiens 4-11 12837278-7 2003 Since the phosphorylation at Ser-3 inactivates the actin-depolymerizing activity of cofilin, these results suggest that NRK/NESK induces actin polymerization through cofilin phosphorylation. Serine 29-32 cofilin 1 Homo sapiens 84-91 12837278-7 2003 Since the phosphorylation at Ser-3 inactivates the actin-depolymerizing activity of cofilin, these results suggest that NRK/NESK induces actin polymerization through cofilin phosphorylation. Serine 29-32 cofilin 1 Homo sapiens 166-173 12655149-3 2003 The activity of cofilin is negatively regulated by phosphorylation at Ser-3. Serine 70-73 cofilin 1 Homo sapiens 16-23 10644754-0 2000 A protein kinase from neutrophils that specifically recognizes Ser-3 in cofilin. Serine 63-66 cofilin 1 Homo sapiens 72-79 11784854-2 2002 LIM kinase 1 (LIMK1) phosphorylates cofilin, an actin-depolymerizing and -severing protein, at Ser-3 and regulates actin reorganization. Serine 95-98 cofilin 1 Homo sapiens 36-43 11784854-8 2002 We used a cell-permeable peptide (S3 peptide) that contains the phosphorylation site (Ser-3) of cofilin to inhibit the cellular function of LIMK1. Serine 86-89 cofilin 1 Homo sapiens 96-103 11418599-3 2001 Like TESK1, TESK2 phosphorylated cofilin specifically at Ser-3 and induced formation of actin stress fibers and focal adhesions. Serine 57-60 cofilin 1 Homo sapiens 33-40 11294912-2 2001 Like LIM-kinases, TESK1 phosphorylated cofilin specifically at Ser-3, both in vitro and in vivo. Serine 63-66 cofilin 1 Homo sapiens 39-46 11171090-3 2001 We report here that LIMK1 and LIMK2 phosphorylate both cofilin and actin-depolymerizing factor (ADF) specifically at Ser-3 and exhibit partially distinct substrate specificity when tested using site-directed cofilin mutants as substrates. Serine 117-120 cofilin 1 Homo sapiens 55-62 11093160-4 2000 The subcellular localization as well as the actin-binding activity of cofilin are regulated by the phosphorylation state of serine-3. Serine 124-130 cofilin 1 Homo sapiens 70-77 12451591-1 2003 The signal transduction pathways that trigger dephosphorylation of cofilin in neutrophils stimulated with the chemoattractant fMet-Leu-Phe (fMLP) were investigated with a phospho-specific antibody that recognized cofilin only when this protein was phosphorylated on ser-3. Serine 266-269 cofilin 1 Homo sapiens 67-74 11890784-2 2002 A key phosphorylatable serine in cofilin, an F-actin cleaving protein, was replaced with a nonphosphorylatable cysteine. Serine 23-29 cofilin 1 Homo sapiens 33-40 10644754-2 2000 Phosphorylation of cofilin on serine residue 3 is known to block these activities. Serine 30-36 cofilin 1 Homo sapiens 19-26 10644754-3 2000 We now report that neutrophils contain a protein kinase that selectively catalyzes the phosphorylation of cofilin on serine 3 (>/=70%) and a nonspecific kinase that recognizes multiple sites in this protein. Serine 117-123 cofilin 1 Homo sapiens 106-113 10644754-9 2000 Thus, neutrophils contain a protein kinase distinct from LIM kinase-1/2 that selectively recognizes serine 3 in cofilin. Serine 100-106 cofilin 1 Homo sapiens 112-119 9655398-4 1998 Here we show that LIM-kinase 1 (LIMK-1), a serine/threonine kinase containing LIM and PDZ domains, phosphorylates cofilin at Ser 3, both in vitro and in vivo. Serine 125-128 cofilin 1 Homo sapiens 114-121 9655398-3 1998 Cofilin is known to be a potent regulator of actin filament dynamics, and its ability to bind and depolymerize actin is abolished by phosphorylation of serine residue at 3; however, the kinases responsible for this phosphorylation have not been identified. Serine 152-158 cofilin 1 Homo sapiens 0-7 10464255-5 1999 Gelsolin, which severs actin filaments, is activated by calcium, whereas the actin disassembly factor cofilin is inhibited by serine phosphorylation. Serine 126-132 cofilin 1 Homo sapiens 102-109 8037689-10 1994 Platelet cofilin was phosphorylated exclusively on serine. Serine 51-57 cofilin 1 Homo sapiens 9-16 33336885-3 2021 Additionally, up-regulated cofilin-1 mainly existed in the serine-3 phosphorylated form, according to the 2D gel immunoblotting assay. Serine 59-65 cofilin 1 Homo sapiens 27-36 34639067-5 2021 Phosphorylation at Ser-3 by kinases attenuate cofilin"s actin-binding activity. Serine 19-22 cofilin 1 Homo sapiens 46-53 34639067-6 2021 In contrast, dephosphorylation at Ser-3 enhances cofilin-induced actin depolymerization. Serine 34-37 cofilin 1 Homo sapiens 49-56 32863228-3 2020 Cofilin activity is mainly regulated by phosphorylation on serine residue 3 making this post-translational modification key to the regulation of myofilament integrity. Serine 59-65 cofilin 1 Homo sapiens 0-7 30550596-7 2018 In addition, after a pharmacological inhibition of LIM kinases, a residual cofilin phosphorylation is observed on serine 3. Serine 114-120 cofilin 1 Homo sapiens 75-82 30115939-5 2018 CFL1 is also phosphorylated by testis-specific kinase 1 (TESK1) on the same serine residue. Serine 76-82 cofilin 1 Homo sapiens 0-4 28939776-2 2017 Phosphorylation of vertebrate cofilin at Ser-3 regulates both actin binding and severing. Serine 41-44 cofilin 1 Homo sapiens 30-37 28939776-8 2017 Third, Ser-3 modification (i.e. substitution with Asp or phosphorylation) "undocks" and repositions the cofilin N terminus away from the filament axis, which compromises S3D cofilin"s ability to weaken longitudinal filament subunit interactions. Serine 7-10 cofilin 1 Homo sapiens 104-111 28939776-8 2017 Third, Ser-3 modification (i.e. substitution with Asp or phosphorylation) "undocks" and repositions the cofilin N terminus away from the filament axis, which compromises S3D cofilin"s ability to weaken longitudinal filament subunit interactions. Serine 7-10 cofilin 1 Homo sapiens 174-181 28939776-9 2017 Collectively, our results demonstrate that, in addition to inhibiting actin binding, Ser-3 modification favors formation of a cofilin-binding mode that is unable to sufficiently alter filament mechanical properties and promote severing. Serine 85-88 cofilin 1 Homo sapiens 126-133 27462783-9 2016 Additionally, MIEN1 promotes cellular adhesion and actin dynamics by inducing phosphorylation of FAK at Tyr-925 and reducing phosphorylation of cofilin at Ser-3, which results in breast cancer cell migration. Serine 155-158 cofilin 1 Homo sapiens 144-151 25998423-3 2015 Cofilin, a protein that controls actin dynamics, is activated by Slingshot phosphatase-dependent serine 3 dephosphorylation by redox-dependent mechanisms. Serine 97-103 cofilin 1 Homo sapiens 0-7 25684665-7 2015 Loss of SSH1L expression was associated with an increase in the phosphorylation of cofilin-1 at serine-3 and further inhibited cell migration (but not proliferation) in KLM1, PANC-1 and MIAPaCa-2. Serine 96-102 cofilin 1 Homo sapiens 83-92 25864508-4 2015 Cofilin is regulated by cofilin binding molecules, is phosphorylated at Ser-3 (inactivation) by LIM-kinases (LIMKs) and testicular protein kinases (TESKs), and is dephosphorylated (reactivation) by slingshot protein phosphatases (SSHs). Serine 72-75 cofilin 1 Homo sapiens 0-7 30550596-8 2018 Interestingly, this 2D gel based proteomic study identified new phosphorylation sites on cofilin, such as threonine 63, tyrosine 82 and serine 108. Serine 136-142 cofilin 1 Homo sapiens 89-96 26269174-6 2015 Cofilin phosphorylation on the serine residue at position 3, an enzymatically inactive form, is increased after MV infection and the phosphorylated form of cofilin is preferentially included in the complex. Serine 31-37 cofilin 1 Homo sapiens 0-7 25595902-6 2015 Only dephosphorylated cofilin (Ser 3) and Drp1 (Ser 637) are translocated to the mitochondria. Serine 31-34 cofilin 1 Homo sapiens 22-29