| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.65313287 |
| Calmodulin binds to the insulin receptor in a Ca2+ dependent manner , whereas it binds to polylysine seemingly by electrostatic interactions . 0.65313287^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Insulin stimulated phosphorylation of calmodulin by rat liver insulin receptor preparations . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| The in vitro phosphorylation of calmodulin by the insulin receptor tyrosine kinase . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| The role of calcium and calmodulin in insulin receptor function in the adipocyte . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| These findings show that the insulin receptor or calmodulin may not be involved in this suppressive effect of W 7 . . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| The IRS proteins , major endogenous targets of the insulin receptor , bind to calmodulin in a Ca ( 2+ ) dependent manner . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Calmodulin is phosphorylated in vitro by the insulin receptor tyrosine kinase and a variety of serine / threonine kinases . ^^^ The ability of the insulin receptor to phosphorylate calmodulin that has been pre phosphorylated by casein kinase 2 is enhanced up to 35 fold , and the sites of phosphorylation on calmodulin are shifted from tyrosine to threonine and serine . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Search for related sequences revealed that the natural inhibitor of the insulin receptor tyrosine kinase [ Auberger , Falquerho , Contreres , Pages , Le Cam , Rossi & Le Cam ( 1989 ) Cell ( Cambridge , Mass . ) 58 , 631 640 ] shows sequence similarity to the mammalian fetuins . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Increasing MgCl 2 from 0 . 5 to 10 mM enhances the phosphorylation of calmodulin catalyzed by the insulin receptor but also reduces the inhibition seen with 500 microM GTP gamma S . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| In a cell free system , tubulin , microtubule associated protein 2 , tau , fodrin , calmodulin dependent kinase , calmodulin , and lipocortins 1 and 2 were reported to be good substrates for insulin receptor kinase . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of calmodulin by the insulin receptor kinase was also inhibited by 1 mM GTP [ S ] both in the absence ( by 88 % ) and in the presence ( by 81 % ) of insulin . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| We present data from several phosphoproteins including calcium calmodulin dependent protein kinase , the beta subunit of the insulin receptor , and phosphorylated calmodulin to demonstrate the utility of this procedure . . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| In vitro tyrosine phosphorylation studies on RAS proteins and calmodulin suggest that polylysine like basic peptides or domains may be involved in interactions between insulin receptor kinase and its substrate . ^^^ Since the tyrosine phosphorylation of calmodulin by the insulin receptor kinase in vitro requires cofactors such as protamine and poly ( L lysine ) , we examined the possibility that poly ( L lysine ) may also potentiate the interaction between RAS proteins and the insulin receptor . ^^^ Further examination of the role of poly ( L lysine ) in potentiating tyrosine phosphorylation of the HRAS protein and calmodulin by purified insulin receptor kinase indicates that poly ( L lysine ) affects the conformation of these protein substrates as well as that of the receptor kinase domain . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Since the studies on tyrosine phosphorylation of calmodulin by the insulin receptor kinase in vitro suggested that protamine and poly ( L lysine ) may activate phosphorylation of the receptor beta subunit [ Sacks & McDonald ( 1988 ) J . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| The carboxyl terminal segment of the c Ki ras 2 gene product mediates insulin stimulated phosphorylation of calmodulin and stimulates insulin independent autophosphorylation of the insulin receptor . ^^^ The highly basic carboxyl terminus of the human c Ki ras 2 gene product stimulated both the in vitro phosphorylation of calmodulin and autophosphorylation of the beta subunit of the insulin receptor , independently of insulin . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Characteristics of calmodulin phosphorylation by the insulin receptor kinase . ^^^ Calmodulin is a substrate for the insulin receptor kinase . ^^^ The time sequence of events resulting in insulin stimulated phosphorylation of calmodulin was analyzed at a number of different insulin concentrations using partially purified solubilized insulin receptor preparations from rat adipocytes . ^^^ The respective insulin concentrations needed to reach half maximal binding , phosphorylation of the beta subunit of the insulin receptor , and phosphorylation of calmodulin were 4 . 5 10 10 ( 10 ) , 4 . 3 10 10 ( 10 ) , and 3 . 9 10 10 ( 10 ) M , respectively . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Purified calmodulin dependent protein phosphatase was shown to catalyse the complete dephosphorylation of phosphotyrosyl ( insulin receptor ) . ^^^ When compared at similar concentrations , 32P labelled EGF receptor was dephosphorylated at greater than 3 times the rate of 32P labelled insulin receptor ; both dephosphorylations exhibited similar dependence on metal ions and calmodulin . ^^^ It is concluded that in cell extracts phosphotyrosyl protein phosphatases other than calmodulin dependent protein phosphatase are the major phosphotyrosyl ( insulin receptor ) and ( EGF receptor ) phosphatases . . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Insulin receptor capping and its correlation with calmodulin dependent myosin light chain kinase . ^^^ Our data indicate that the calmodulin dependent myosin light chain kinase may be directly responsible for the activation of actomyosin mediated contractility during insulin receptor capping . . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| The 32Pi incorporated into calmodulin was stable to base , indicating that phosphotyrosine was involved and thus implicating the insulin receptor tyrosine kinase as being responsible for its phosphorylation . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| By contrast , the insulin receptor kinase catalyzed the phosphorylation of the calmodulin dependent kinase and addition of insulin in vitro resulted in a 40 % increase in this phosphorylation . ^^^ In the presence of calmodulin dependent kinase and the insulin receptor kinase , insulin also stimulated the phosphorylation of calmodulin . ^^^ These data suggest that the insulin receptor kinase may interact directly and specifically with the calmodulin dependent kinase and calmodulin . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Using immunocytochemical techniques , we determined that actin , myosin , calmodulin and myosin light chain kinase ( MLCK ) are all accumulated directly underneath insulin receptor caps . ^^^ Furthermore , a number of drugs known to abolish the activation properties of calmodulin , such as trifluoperazine ( TFP ) or W 7 , strongly inhibit insulin receptor capping and myosin light chain phosphorylation . ^^^ These data imply that an actomyosin cytoskeletal contraction , regulated by Ca2+ / calmodulin and MLCK , is involved in insulin receptor capping . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| The insulin receptor and calmodulin . ^^^ In this investigation , we demonstrate that calmodulin enhances insulin stimulated phosphorylation of the beta subunit of the insulin receptor and histone H2b and that insulin also stimulates phosphorylation of calmodulin . ^^^ Using wheat germ lectin enriched insulin receptor preparations obtained from rat adipocyte plasma membranes , calmodulin stimulated the rate and increased the amount of 32P incorporated predominantly into tyrosine residues of the beta subunit of the receptor when assayed in the presence of insulin . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| The insulin receptor contains a calmodulin binding domain . ^^^ Because binding of insulin to its receptor represents the initial site of insulin action in the plasma membrane , studies were undertaken to determine whether the insulin receptor is a calmodulin binding protein . ^^^ Preparations enriched in the insulin receptor and calmodulin binding proteins were isolated from detergent solubilized rat adipocyte membranes by chromatography with wheat germ agglutinin agarose and calmodulin conjugated Sepharose , respectively . ^^^ Binding and photocovalent cross linking of iodine 125 labeled calmodulin to these affinity purified preparations and to isolated plasma membranes , followed by immunoadsorption with insulin receptor antibodies bound to protein A Sepharose , resulted in significant purification of a binding complex of 110K to 140K . ^^^ These results indicate that the adipocyte insulin receptor or a polypeptide closely associated with the receptor is a calmodulin binding protein . . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| It is suggested that insulin receptor phosphorylation is an energy requiring process that is Ca2+ dependent and may be modulated by calmodulin . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| In contrast , calmodulin phosphorylated on tyrosine residues by the insulin receptor kinase produced an increase in the Vmax , with no alteration in the affinity for CaM kinase 2 or the K0 . 5 for Ca2+ . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Calmodulin is phosphorylated by the purified insulin receptor on tyrosine residues with a maximum stoichiometry of 1 mol phosphate / mol of calmodulin . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Two dimensional phosphopeptide mapping of calmodulin immunoprecipitated from rat hepatocytes and calmodulin phosphorylated in vitro by the insulin receptor kinase or casein kinase 2 revealed several common phosphopeptides . ^^^ The common phosphopeptides that appeared insulin sensitive in intact cells comprised 61 and 40 % of casein kinase 2 and insulin receptor catalyzed 32P incorporation into calmodulin in vitro , respectively . ^^^ This suggests that casein kinase 2 and the insulin receptor kinase are , at least in part , responsible for insulin stimulated phosphorylation of calmodulin in rat hepatocytes . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| The role of polybasic compounds in determining the tyrosyl phosphorylation of calmodulin by the human insulin receptor . ^^^ A highly purified human insulin receptor preparation was shown to effect receptor autophosphorylation and the phosphorylation of poly ( GluTyr ) but not that of calmodulin . ^^^ Polybasic substances such as poly L arginine , histone H 1 and protamine sulphate all promoted calmodulin phosphorylation by the insulin receptor in a similar biphasic dose dependent fashion . ^^^ It is suggested that calmodulin can be phosphorylated by the insulin receptor only when it is cross linked in a multivalent fashion to a suitable polybasic substance so that it forms large multimeric aggregates . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| The effects of specific anti calmodulin monoclonal antibodies on the conformation and interaction of calmodulin with two enzymes , the insulin receptor tyrosine kinase and casein kinase 2 , are examined . ^^^ In contrast , two other anti calmodulin monoclonal antibodies , 4F4 and 4G2 , decrease phosphorylation of calmodulin by both the insulin receptor kinase and casein kinase 2 . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Additionally , polylysine , a polycation postulated to interact with the insulin receptor beta subunit acidic domain , increased autophosphorylation and facilitated insulin induced phosphorylation of calmodulin in the wild type as well as the hIR 1262 receptors . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| Phosphocalmodulin immunoprecipitated from control and insulin treated CHO / IR cells , and calmodulin phosphorylated in vitro by the insulin receptor kinase and casein kinase 2 were resolved by two dimensional phosphopeptide mapping . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| In contrast , tyrosine phosphorylation of mammalian calmodulin by the insulin receptor kinase did not significantly alter calmodulin stimulated Ca ( 2+ ) ATPase activity . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| In summary , CaM phosphorylation by MLCK differs from CaM phosphorylation catalyzed by other kinases ( i . e . , the insulin receptor or casein kinase 2 ) in both basic peptide and Ca2+ requirements as well as in the sites of phosphorylation . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| CDK2 / cyclin A , insulin receptor tyrosine kinase and MAPK ) ; kinases in the active state ( e . g . casein kinase 1 , Lck ) ; and kinases in inactive states ( e . g . twitchin kinase , calcium calmodulin kinase 1 , FGF receptor kinase , c Src and Hck ) . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| We found 6 proteins not previously known to be substrates of CaM kinase 2 , namely PSD 95 associated protein , SAP 97 , TOAD 64 , TNF receptor associated protein , insulin receptor tyrosine kinase 58 / 53 kDa substrate , and homer 1b . . ^^^ |
|
| Interacting proteins: P06213 and P62158 |
Pubmed |
SVM Score :0.0 |
| On the other hand , within the protein tyrosine kinases involved in the phosphorylation of CaM are receptors with tyrosine kinase activity , such as the insulin receptor and the epidermal growth factor receptor , and nonreceptor protein tyrosine kinases , such as several members of the Src family kinases , Janus kinase 2 , and p38Syk . ^^^ |
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