Phosphorylation of fodrin (nonerythroid spectrin) by the purified insulin receptor kinase

Kadowaki, Takashi; Nishida, Eisuke; Kasuga, Masato; Akiyama, Tetsu; Takaku, Fumimaro; Ishikawa, Masashi; Sakai, Hikoichi; Kathuria, S. P.; Fujita‐Yamaguchi, Yoko

doi:10.1016/s0006-291x(85)80187-x

Cited by 38 publications

(26 citation statements)

References 22 publications

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“…15 The inability of Manno et al 6 to detect β-spectrin reactivity with anti-phosphotyrosine antibody is probably due to the lower concentration of vanadate present in their ghost preparation (10 µM) compared to this study (1 mM).…”

Section: Discussioncontrasting

confidence: 51%

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Tohtong¹,

Metheenukul²,

Wilairat³

2002

ScienceAsia

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The steady-state levels of β-spectrin phosphorylation in HbH (α-thalassemia 1/α-thalassemia 2), HbH/HbConstant Spring (α-thalassemia 1/HbCS, hereafter called HbH/HbCS) and nonsplenectomized β-thalassemia/HbE (hereafter called β-thal/HbE) red cells were quantitated using Western hybridization. Phosphorylation of β-spectrin serine and threonine residues from thalassemic samples was not significantly different from normal control. However, tyrosine phosphorylation was higher than normal control in HbH (p<0.01), HbH/HbCS (p<0.05) and β-thal/HbE (p<0.05) samples. Tyrosine phosphorylation of β-spectrin was observed only in the presence of vanadate, a phenomenon not hitherto reported. As tyrosine kinase activity has been linked to oxidative stress, loss of membrane lipid asymmetry and procoagulant activity of the red cell membrane, the observed increase in β-spectrin tyrosine phosphorylation of the thalassemic red cells is likely, at least in part, to account for these parameters.

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Section: Discussioncontrasting

confidence: 51%

Untitled

Tohtong¹,

Metheenukul²,

Wilairat³

2002

ScienceAsia

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“…Although the molecular nature of this association awaits further investigation, these data suggest that Ror receptors may interact either directly or indirectly with neuronal microtubules and/or actin microfilaments. Interestingly, a number of receptor kinases have been shown to bind to cytoskeletal proteins and modulate their functional properties (Kadowaki et al, 1985;Nishida et al, 1987;Carman et al, 1998).…”

Section: P<0mentioning

confidence: 99%

Neurite extension in central neurons: a novel role for the receptor tyrosine kinases Ror1 and Ror2

Paganoni

Ferreira

2005

Journal of Cell Science

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Neurite elongation and branching are key cellular events during brain development as they underlie the formation of a properly wired neuronal network. Here we report that the receptor tyrosine kinases Ror1 and Ror2 modulate the growth of neurites as well as their branching pattern in hippocampal neurons. Upon Ror1 or Ror2 suppression using antisense oligonucleotides or RNA interference (RNAi), neurons extended shorter and less branched minor processes when compared to those in control cells. In addition, Ror-depleted cells elongated longer, albeit less branched, axons than seen in control cells. Conversely, Ror overexpression both in non-neuronal cells and in hippocampal neurons resulted in the enhanced extension of short and highly branched processes. These phenotypes were accompanied by changes in the microtubule-associated proteins MAP1B and MAP2. Taken together, these results support a novel role for Ror receptors as modulators of neurite extension in central neurons.

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“…Less clear is whether spectrin can be tyrosine-phosphorylated and whether the ␣-subunit of spectrin is ever covalently phosphorylated. One report indicates that ␤-spectrin can be tyrosine-phosphorylated when incubated in vitro with purified insulin receptor kinase (12). Another report has appeared indicating that both spectrin subunits are tyrosine-phosphorylated when incubated in vitro with a spleen protein tyrosine kinase (13).…”

mentioning

confidence: 99%

c-Src Binds αII Spectrin's Src Homology 3 (SH3) Domain and Blocks Calpain Susceptibility by Phosphorylating Tyr1176

Nedrelow

Cianci

Morrow

2003

Journal of Biological Chemistry

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Spectrin is a ubiquitous heterodimeric scaffolding protein that stabilizes membranes and organizes protein and lipid microdomains on both the plasma membrane and intracellular organelles. Phosphorylation of ␤-spectrin on Ser/Thr is well recognized. Less clear is whether ␣-spectrin is phosphorylated in vivo and whether spectrin is phosphorylated on tyrosine (pTyr). We affirmatively answer both questions. In cultured Madin-Darby canine kidney cells, ␣II spectrin undergoes in vivo tyrosine phosphorylation. Enhancement of the steady state level of pTyr-modified ␣II spectrin by vanadate, a phosphatase inhibitor, implies a dynamic balance between ␣II spectrin phosphorylation and dephosphorylation. Recombinant peptides containing the Src homology 3 domain of ␣II spectrin (but not the Src homology 3 domain of ␣I spectrin) bind specifically to phosphorylated c-Src in Madin-Darby canine kidney cell lysates, suggesting that this kinase is responsible for its in vivo phosphorylation. pTyr-modified ␣II spectrin is resistant to maitotoxin-induced cleavage by -calpain in vivo. In vitro studies of recombinant ␣II spectrin peptides representing repeats 9 -12 identify two sites of pTyr modification. The first site is at Tyr 1073 , a residue immediately adjacent to a region encoded by alternative exon usage (insert 1). The second site is at Tyr 1176 . This residue flanks the major site of cleavage by the calciumdependent protease calpain, and phosphorylation of Tyr 1176 by c-Src reduces the susceptibility of ␣II spectrin to cleavage by -calpain. Calpain cleavage of spectrin, activated by Ca 2؉ and calmodulin, contributes to diverse cellular processes including synaptic remodeling, receptor-mediated endocytosis, apoptosis, and the response of the renal epithelial cell to ischemic injury. Tyrosine phosphorylation of ␣II spectrin now would appear to also mediate these events. The spectrin skeleton thus forms a point of convergence between kinase/phosphatase and Ca 2؉ -mediated signaling cascades.

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Phosphorylation of fodrin (nonerythroid spectrin) by the purified insulin receptor kinase

Cited by 38 publications

References 22 publications

Untitled

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Neurite extension in central neurons: a novel role for the receptor tyrosine kinases Ror1 and Ror2

c-Src Binds αII Spectrin's Src Homology 3 (SH3) Domain and Blocks Calpain Susceptibility by Phosphorylating Tyr1176

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