Involvement of protein kinase C in the regulation of assembly-disassembly of neurofilaments in vitro

Gonda, Y; Nishizawa, Kunihide; Ando, Shoji; Kitamura, Shinobu; Minoura, Yasushi; Nishi, Yoshimi; Inagaki, Masaki

doi:10.1016/0006-291x(90)90667-c

Cited by 85 publications

(53 citation statements)

References 25 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: 99%

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

1999

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Section: Discussionmentioning

confidence: 99%

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

1999

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“…Similar data were obtained in the cases of other IF proteins. All the phosphorylation sites on GFAP by A kina~e(l~83~), C kinase (15) and CaMKII(16), on desmin by A kinase("~~~), C k i n a~e (~~) and cdc2 kinase(18), on keratin 8 by A kinase (S. Ando et al, unpublished data), and on NF-L by A k i n a~e (~~) and C kinase (22) are located in head domains, except for Ser389 of GFAP and Ser416 of keratin 8 (Table 2). Together with data obtained by mutagenesis analysis that the head domains play key roles in IF a~s e r n b l y (~~-~~) , these results indicate that phosphorylation of the head domains is responsible for disassembly of these IFs.…”

Section: In Vitro Disassembly Of Ifs By Phosphorylationmentioning

confidence: 96%

“…Analysis of tryptic phosphopeptide maps showed that the sites of phosphorylation by A kinase and by C kinase differ, which in turn suggests that phosphorylations by these kinases are sitespecific. Subsequently, similar in vitro disassembly of the filament structure by protein kinases was noted for almost all major types of IF protein, namely ~imentin(~-'~), glial fibrillary acidic protein (GFAP) (15- (21)(22)(23) and lamin (24)(25)(26)(27)(28) (Table 1). Interestingly, each IF protein underwent disassembly by phosphorylation in the presence of distinct kinases (Table 1).…”

Section: In Vitro Disassembly Of Ifs By Phosphorylationmentioning

confidence: 97%

Dynamic property of intermediate filaments: Regulation by phosphorylation

et al. 1996

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SummarySite-specific phosphorylation of intermediate filament (IF) proteins on serine and threonine residues leads to alteration of the filament structure, in vitro and in vivo. Protein kinases involved in cell signaling and those activated in mitosis dynamically control spatial and temporal organization of intracellular IF phosphorylation. Thus, IF phosphorylation appears to be one of the most predominant strategies in coordinating intracellular organization of the IF Accepted 6 March 1996 network.

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“…The mechanism of NF-assembly therefore remains to be elucidated. It has been shown in vitro that phosphorylation of NF-L by the catalytic subunit of cAMP-dependent protein kinase (A-kinase) and protein kinase C inhibited its polymerization into long filaments and also depolymerized filaments (Gonda et al, 1990;Nakamura et al, 1990). The major A-kinase phosphorylation site has been identified as Ser-55 in the amino-terminal head domain of NF-L (Sihag and Nixon, 1991).…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of native and reassembled neurofilaments composed of NF-L, NF-M, and NF-H by the catalytic subunit of cAMP-dependent protein kinase.

Hisanaga

Matsuoka

Nishizawa

et al. 1994

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native NF was nearly the same as that of purified NF-L. However, phosphorylation did not cause the native NFs to disassemble into oligomers, as was the case for purified NF-L. Instead, partial fragmentation was detected in sedimentation experiments and by electron microscopic observations. This is probably not due to the presence of the three NF subunits in NF or to differences in phosphorylation sites because reassembled NF containing all three NF subunits were disassembled into oligomeric forms by phosphorylation with A-kinase and the phosphorylation by A-kinase occurred at the head domain of NF-L whether NF were native or reassembled. Disassembling intermediates of reassembled NF containing all three NF subunits were somewhat different from disassembling intermediates of NF-L. Thinning and loosening of filaments was frequently observed preceding complete disassembly. From the fact that the thinning was also observed in the native filaments phosphorylated by A-kinase, it is reasonable to propose the native NF is fragmented through a process of thinning that is stimulated by phosphorylation in the head domain of the NF subunits.

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Involvement of protein kinase C in the regulation of assembly-disassembly of neurofilaments in vitro

Cited by 85 publications

References 25 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

Dynamic property of intermediate filaments: Regulation by phosphorylation

Phosphorylation of native and reassembled neurofilaments composed of NF-L, NF-M, and NF-H by the catalytic subunit of cAMP-dependent protein kinase.

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