The identification of a new actin-binding region in p57

Liu, Changzhen; Chen, Yong; Sui, Sen-Fang

doi:10.1038/sj.cr.7310014

Cited by 20 publications

(10 citation statements)

References 24 publications

(40 reference statements)

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“…Previous studies indicated that full-length CRN2 possesses binding sites for F-actin in the conserved WD40-repeat domain forming the seven-bladed β-propeller659 and in the conserved part of the C-terminal linker region34596061. More specifically, a conserved arginine residue, R30 in CRN1 and R28 in CRN2, which is surface exposed and located within the seventh β-propeller blade3, has turned out to be essential for F-actin binding of both coronin proteins1262.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration

Xavier

Rastetter

Blomacher

et al. 2012

Sci Rep

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CRN2 (synonyms: coronin 1C, coronin 3) functions in the re-organization of the actin network and is implicated in cellular processes like protrusion formation, secretion, migration and invasion. We demonstrate that CRN2 is a binding partner and substrate of protein kinase CK2, which phosphorylates CRN2 at S463 in its C-terminal coiled coil domain. Phosphomimetic S463D CRN2 loses the wild-type CRN2 ability to inhibit actin polymerization, to bundle F-actin, and to bind to the Arp2/3 complex. As a consequence, S463D mutant CRN2 changes the morphology of the F-actin network in the front of lamellipodia. Our data imply that CK2-dependent phosphorylation of CRN2 is involved in the modulation of the local morphology of complex actin structures and thereby inhibits cell migration.

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Section: Discussionmentioning

confidence: 99%

Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration

Xavier

Rastetter

Blomacher

et al. 2012

Sci Rep

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“…Our findings are similar to the actin-binding mechanism of CORO1A (also known as coronin-like protein p57), a member of the coronin family. F-actin-binding of CORO1A through the C-terminus (CT, 297-461) requires a functional leucine zipper situated in a short dimerization/ trimerization domain (CC, 432-461) (Liu et al, 2006). In addition to the direct F-actin binding, coupling of CMS or CIN85 to F-actin via cortactin (Lynch et al, 2003), Alix/AIP1 (Chen et al, 2000), or CapZ (Hutchings et al, 2003) adds a layer of complexity and probably regulation.…”

Section: Discussionmentioning

confidence: 99%

Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation

Gaidos

Soni

Oswald

et al. 2007

Journal of Cell Science

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Members of the CMS/CIN85 protein family participate in clathrin-mediated endocytosis and play a crucial role in maintaining the kidney filtration barrier. The CMS protein structure includes three Src homology 3 (SH3) domains and a proline-rich (PR) region that is connected by a `linker' sequence to a coiled-coil (CC) domain. We show that CMS is a component of special actin-rich adhesion structures – podosomes – and demonstrate specific actin-binding properties of CMS. We have found that the entire C-terminal half of CMS is necessary for efficient binding to filamentous actin (F-actin). CMS and CIN85 can crosslink F-actin into bundles, a function that depends on the PR region and the CC domain. Removal of these domains reduces migration. CMS can also form heterotypic complexes with CIN85. CIN85 is expressed as multiple isoforms that share the CC domain, suggesting that heterotypic interactions with CMS provides a mechanism to regulate CMS binding to F-actin and thus for modulating dynamic rearrangements of the cytoskeleton.

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“…This structure includes two cryptic blades that flank the five known WD40 repeats and a Cterminal extension that folds tightly along the bottom of the ␤-propeller. Many of the earlier attempts to map the F-actinbinding site of coronin used truncation mutants that contained fragments of this compact structure (Gatfield et al, 2005;Liu et al, 2006;Mishima and Nishida, 1999;Oku et al, 2003;Spoerl et al, 2002). These fragments may not adopt stable or physiological conformations and the results of these studies must be confirmed using mutations in the full-length protein (Appleton et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

F-actin binding is essential for coronin 1B function in vivo

Cai

Makhov

Bear

2007

Journal of Cell Science

108

111

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Coronins are conserved F-actin binding proteins that have been implicated in a variety of processes including fibroblast migration, phagocytosis, and chemotaxis. Recent data from our lab indicate that coronin 1B coordinates Arp2/3-dependent actin filament nucleation and cofilin-mediated filament turnover at the leading edge of migrating fibroblasts. Analysis of coronin function has been hampered by the lack of a clear understanding of how coronin interacts with F-actin. Here, we identify a surface-exposed conserved arginine residue at position 30 (R30), which is crucial for coronin 1B binding to F-actin both in vitro and in vivo. Using actin co-sedimentation, we demonstrate that coronin 1B binds with high affinity to ATP/ADP-Pi–F-actin (170 nM) and with 47-fold lower affinity to ADP–F-actin (8 μM). In contrast to a previous study, we find no evidence for enhanced cofilin binding to F-actin in the presence of either coronin 1B or coronin 1A. Instead, we find that coronin 1B protects actin filaments from cofilin-induced depolymerization. Consistent with an important role for interactions between coronin 1B and F-actin in vivo, an R30D coronin mutant that does not bind F-actin localizes inefficiently to the leading edge. Furthermore, our analysis indicates that F-actin binding is absolutely required for coronin 1B to exert its effects on whole-cell motility and lamellipodial dynamics.

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The identification of a new actin-binding region in p57

Cited by 20 publications

References 24 publications

Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration

Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration

Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation

F-actin binding is essential for coronin 1B function in vivo

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