Casein kinases I and II from squid brain exhibit selective neurofilament phosphorylation

Link, William T.; Grant, Philip; Hidaka, Hiroyoshi; Pant, Harish C.

doi:10.1016/1044-7431(92)90067-c

Cited by 12 publications

(6 citation statements)

References 30 publications

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“…For example, second messenger-dependent (PKA, PKC) and independent kinases (CKI) copurify with NFs (Docemeci and Pant, 1992;Sihag et al, 1988;Nixon, 1989, 1990;Gonda et al, 1990;Julien et al, 1983;Toru-Delbauffe et al, 1983;Caputo et al, 1989;Docemeci et al, 1990;Floyd et al, 1991;Link et al, 1992). In addition proline-directed kinases such as cdc2-like kinases (Shetty et al, 1993;Starr et al, 1997;Takahashi et al, 1995), cdk5 (Lew et al, 1992;Lee and Johnston, 1997) and MAP kinases (Runge et al, 1981;Roder and Ingram, 1991;Roder et al, 1993) also coassemble with NFs.…”

Section: Discussionmentioning

confidence: 97%

“…Previous studies have shown that casein kinase I (CKI ) is primarily responsible for the endogenous phosphorylation of NF220 in an NF preparation obtained from axoplasm and squid brain (optic lobes) (Floyd et al, 1991;Link et al, 1992). CKI selectively associates with and actively phosphorylates NF220 in both preparations.…”

Section: Axoplasm and Gfl Extracts Contain Similar Levels Of Kinase Amentioning

confidence: 97%

“…residues, while NFs are transported in axons and assembled into a cytoskeleton (Oblinger, 1987;Shetty et al, 1993;Lee and Cleveland, 1996;Link et al, 1992;Hollander et al, 1996;Guidato et al, 1996;Roder and Ingram, 1991;Roder et al, 1993;Giasson and Mushynski, 1996;Veeranna et al, 1998;Lew et al, 1992;Starr et al, 1996). Phosphorylation of the KSP repeats induces sidearm formation and mutual interactions among neurofilaments and other cytoskeletal proteins (e.g., microtubules) (Hirokawa, 1991;, which organize into a dynamic cytoskeletal lattice that expands axon caliber (Hoffman, 1995;deWaegh et al, 1992).…”

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confidence: 96%

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Topographic regulation of cytoskeletal protein phosphorylation by multimeric complexes in the squid giant fiber system

1999

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Section: Discussionmentioning

confidence: 97%

Section: Axoplasm and Gfl Extracts Contain Similar Levels Of Kinase Amentioning

confidence: 97%

mentioning

confidence: 96%

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Topographic regulation of cytoskeletal protein phosphorylation by multimeric complexes in the squid giant fiber system

1999

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“…Kinases regulating neurofilament dynamics include cyclindependent protein kinase 5 (CDK5), mitogen-activated protein kinases (MAPKs), casein kinase 1 and 2 (CK1 and CK2), glycogen synthase kinase 3a and 3b (GSK3a and GSK3b), p38 MAPK and cJun terminal kinase (JNK) (Guan et al, 1991;Link et al, 1992;Guidato et al, 1996;Bajaj and Miller, 1997;Giasson and Mushynski, 1997;Veeranna et al, 1998;Bajaj et al, 1999;Li et al, 1999;Ackerley et al, 2000;Ackerley et al, 2003;Kesavapany et al, 2003;Waetzig and Herdegen, 2003;Chan et al, 2004;Barry et al, 2007;DeFuria and Shea, 2007;Perrot et al, 2008;Holmgren et al, 2012). Phosphatases that regulate neurofilament dynamics include protein phosphatase 1, 2A and 2B (PP1, PP2A and PP2B) (Shea et al, 1993;Saito et al, 1995;Strack et al, 1997;Jung and Shea, 1999;Gong et al, 2003;Veeranna et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Divergent and convergent roles for kinases and phosphatases in neurofilament dynamics

Lee

Pant²,

Shea

2014

Journal of Cell Science

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C-terminal neurofilament phosphorylation mediates cation-dependent self-association leading to neurofilament incorporation into the stationary axonal cytoskeleton. Multiple kinases phosphorylate the C-terminal domains of the heavy neurofilament subunit (NF-H), including cyclin-dependent protein kinase 5 (CDK5), mitogenactivated protein kinases (MAPKs), casein kinase 1 and 2 (CK1 and CK2) and glycogen synthase kinase 3b (GSK3b). The respective contributions of these kinases have been confounded because they phosphorylate multiple substrates in addition to neurofilaments and display extensive interaction. Herein, differentiated NB2a/d1 cells were transfected with constructs expressing GFP-tagged NF-H, isolated NF-H sidearms and NF-H lacking the distal-most 187 amino acids. Cultures were treated with roscovitine, PD98059, Li + , D4476, tetrabromobenzotriazole and calyculin, which are active against CDK5, MKK1 (also known as MAP2K1), GSK3b, CK1, CK2 and protein phosphatase 1 (PP1), respectively. Sequential phosphorylation by CDK5 and GSK3b mediated the neurofilamentneurofilament associations. The MAPK pathway (i.e. MKK1 to ERK1/ 2) was found to downregulate GSK3b, and CK1 activated PP1, both of which promoted axonal transport and restricted neurofilamentneurofilament associations to axonal neurites. The MAPK pathway and CDK5, but not CK1 and GSK3b, inhibited neurofilament proteolysis. These findings indicate that phosphorylation of neurofilaments by the proline-directed MAPK pathway and CDK5 counterbalance the impact of phosphorylation of neurofilaments by the non-proline-directed CK1 and GSK3b.

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“…The molecular weights of the four prominent kinases detected by the in situ assay are substantially different from any of the kinases thought to phosphorylate NF, casein kinase I (Floyd et al,199 l), casein kinase II (Link et al, 1992) calcium/calmodulin-dependent kinase (Vallano et al, 1986) cdc or cdk2 kinases (Hisanaga et al, 1991) erk kinases (Drews et al, 1992) the 67 kDa kinase doublet described by Wible et al, (1989), or the 36 and 40 kDa kinases described by Roder and Ingram (199 1). The size and heterogeneity of the kinases were, however, similar to PKC isoforms.…”

Section: Identijication Of Novel Nf-associated Kinases By In Situ Kinmentioning

confidence: 86%

Identification and characterization of a novel (115 kDa) neurofilament- associated kinase

Xiao

Monteiro

1994

J. Neurosci.

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Neurofilaments (NF), the major cytoskeletal component in neuronal cells, are one of the most highly phosphorylated proteins expressed in brain. Apart from the structural role NFs play in maintaining neuronal architecture, little else is known of their function. We describe here evidence suggesting that NF may support many other proteins in the neuronal axoplasm including protein kinases. In order to isolate proteins that bind NF, we first expressed the carboxyl-terminal tail domain of the mouse high-molecular-weight NF subunit (NF-H) as a fusion protein in bacteria and then used this portion of NF-H as a ligand in affinity chromatography. A number of different proteins were isolated from mouse brain lysate that specifically bound to the NF-H column and that did not bind to a control column to which BSA was bound as a ligand. The proteins eluted from the NF-H column contained kinases able to phosphorylate NF proteins efficiently in vitro. We characterized these kinases further by separating proteins on denaturing polyacrylamide gels and reconstituting kinase activity in situ. Using this assay we identified a number of individual kinases including a 115 kDa polypeptide that showed a significant preference for NF proteins as substrate. Native NF was found to be the best substrate for the 115 kDa kinase, followed by a bacterially expressed NF-H nonfusion protein, and NF-H fusion protein. However, low-molecular-weight NF subunit (NF-L) was a poor substrate. Two different NF monoclonal antibodies, SMI31 and SMI32 (Sternberger Monoclonal Inc.), were used to demonstrate further that the 115 kDa kinase is associated with NF in vivo. The kinase was coimmunoprecipitated along with NF by the two NF monoclonal antibodies but appeared to be preferentially associated with phosphorylated forms of NF. We discuss here some of the novel properties of the 115 kDa NF- associated kinase we have termed NAK115 (for NF-associated kinase with a molecular weight of 115 kDa).

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Casein kinases I and II from squid brain exhibit selective neurofilament phosphorylation

Cited by 12 publications

References 30 publications

Topographic regulation of cytoskeletal protein phosphorylation by multimeric complexes in the squid giant fiber system

Topographic regulation of cytoskeletal protein phosphorylation by multimeric complexes in the squid giant fiber system

Divergent and convergent roles for kinases and phosphatases in neurofilament dynamics

Identification and characterization of a novel (115 kDa) neurofilament- associated kinase

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