Oligomeric structure of α-calmodulin-dependent protein kinase II11Edited by A. R. Fersht

Morris, Edward P.; Török, Katalin

doi:10.1006/jmbi.2001.4584

Cited by 80 publications

(81 citation statements)

References 23 publications

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“…Thus, we conclude that in living cells the catalytic domains of the autoinhibited holoenzyme are organized as dimers. (10), or by Kolodziej and colleagues (16). In the first model, catalytic domains are coplanar and spaced evenly around the association domain core.…”

Section: Discussionmentioning

confidence: 99%

“…Each CaMKII subunit is composed of an N-terminal catalytic domain, a regulatory domain, and a C-terminal association domain, that assemble to form a holoenzyme whose structure has been extensively studied in vitro (10)(11)(12)(13)(14)(15). Electron microscopy (EM) imaging of single particles of CaMKII isolated from rat brain revealed ''flower-like'' structures with association domains in a central core and catalytic domains radiating out like petals (15).…”

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confidence: 99%

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Structural rearrangement of CaMKIIα catalytic domains encodes activation

Thaler

Koushik²,

Puhl³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Structural rearrangement of CaMKIIα catalytic domains encodes activation

Thaler

Koushik²,

Puhl³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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“…The crystal structures of the individual domains were known, and there were EM structures of the whole protein (Hoelz et al, 2003;Kolodziej et al, 2000;Morris and Torok, 2001;Rosenberg et al, 2005). CAMKII is a dodecameric enzyme with two hexameric rings formed by a central association domain complex, and the kinase domains are fixed exterior to the central rings.…”

Section: Applications Of Saxs To Structural Analysismentioning

confidence: 99%

Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography

Tsutakawa

Hura

Frankel

et al. 2007

Journal of Structural Biology

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“…The multimeric CaMKII holoenzymes are composed of 12 subunits (Kolodziej et al, 2000;Morris and Torok, 2001;Rosenberg et al, 2005;Rosenberg et al, 2006) of a single isoform or combinations of different isoforms (Bayer et al, 1998;Shen et al, 1998;Brocke et al, 1999;Lantsman and Tombes, 2005). All CaMKII isoforms contain an N-terminal kinase domain and a C-terminal association domain, connected by a variable linker region that is subject to alternative splicing (see Figure 1).…”

Section: Introductionmentioning

confidence: 99%

CaMKIIβ Association with the Actin Cytoskeleton Is Regulated by Alternative Splicing

O’Leary¹,

Lasda²,

Bayer

2006

MBoC

106

127

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The Ca 2؉ /calmodulin (CaM)-dependent protein kinase II (CaMKII)␤ has morphogenic functions in neurons not shared by the ␣ isoform. CaMKII␤ contains three exons (v1, v3, and v4) not present in the CaMKII␣ gene, and two of these exons (v1 and v4) are subject to differential alternative splicing. We show here that CaMKII␤, but not ␣, mediated bundling of F-actin filaments in vitro. Most importantly, inclusion of exon v1 was required for CaMKII␤ association with the F-actin cytoskeleton within cells. CaMKII␤e, which is the dominant variant around birth and lacks exon v1 sequences, failed to associate with F-actin. By contrast, CaMKII␤, which instead lacks exon v4, associated with F-actin as full-length CaMKII␤. Previous studies with CaMKII␤ mutants have indicated a role of nonstimulated kinase activity in enhancing dendritic arborization. Here, we show that F-actin-targeted CaMKII␤, but not ␣, was able to phosphorylate actin in vitro even by nonstimulated basal activity in absence of Ca 2؉ /CaM. In rat pancreatic islets and in skeletal muscle, the actin-associated CaMKII␤ and ␤M were the predominant variants, respectively. Thus, cytoskeletal targeting may mediate functions of CaMKII␤ variants also outside the nervous system. INTRODUCTIONChanges in synaptic connectivity between neurons are widely thought to underlie higher brain functions such as learning and memory and are also important during development. Long-lasting changes in connectivity are often associated with morphological plasticity in structure or number of synaptic connections (for reviews, see Huntley et al., 2002;McGee and Bredt, 2003;Lamprecht and LeDoux, 2004;Segal, 2005). The ␣ isoform of Ca 2ϩ /calmodulin(CaM)-dependent protein kinase II (CaMKII) has been studied extensively because of its prominent role in regulating the strength of individual synaptic connections (for examples, see Malinow et al., 1989;Silva et al., 1992;Giese et al., 1998; for reviews, see Malenka and Nicoll, 1999;Lisman et al., 2002;Griffith, 2004). Much less is known about the other major brain isoform, CaMKII␤. However, CaMKII␤ has specific morphogenic functions in regulating dendritic arborization and synapse density not shared by the ␣ isoform (Fink et al., 2003). This isoform specificity is thought to be mediated by the specific binding of CaMKII␤, but not ␣ to F-actin (Shen et al., 1998;Fink et al., 2003).The four CaMKII isoforms encoded by different genes (␣, ␤, ␥, and ␦) are highly homologous to each other and can phosphorylate and regulate a variety of substrate proteins in response to Ca 2ϩ signals (for reviews, see Soderling et al., 2001;Hudmon and Schulman, 2002;Lisman et al., 2002;Colbran and Brown, 2004). The multimeric CaMKII holoenzymes are composed of 12 subunits (Kolodziej et al., 2000;Morris and Torok, 2001;Rosenberg et al., 2005;Rosenberg et al., 2006) of a single isoform or combinations of different isoforms (Bayer et al., 1998;Shen et al., 1998;Brocke et al., 1999;Lantsman and Tombes, 2005). All CaMKII isoforms contain an N-terminal kinase domain and a ...

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Oligomeric structure of α-calmodulin-dependent protein kinase II11Edited by A. R. Fersht

Cited by 80 publications

References 23 publications

Structural rearrangement of CaMKIIα catalytic domains encodes activation

Structural rearrangement of CaMKIIα catalytic domains encodes activation

Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography

CaMKIIβ Association with the Actin Cytoskeleton Is Regulated by Alternative Splicing

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