Structural basis of the Ca2+-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I

Réty, S.; Osterloh, D.; Arié, Jean Philippe; Tabaries, Sébastien; Seeman, Joachim; Russo‐Marie, Françoise; Gerke, Volker; Lewit-Bentley, Anita

doi:10.1016/s0969-2126(00)00093-9

Cited by 185 publications

(244 citation statements)

References 59 publications

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“…Data were processed using HKL-2000 (Otwinowski & Minor, 1997; see Table 1 for crystallographic statistics). Our data belonged to the same space group (C2) with similar (<1.5 Å difference) unit-cell parameters as the previously reported S100A10-AnxA2 structure (PDB entry 1bt6; Ré ty et al, 1999); phasing was therefore achieved using REFMAC5 (Murshudov et al, 2011) with native S100A10-AnxA2 (Ré ty et al, 2000) as the model. Further refinement and model building were performed using PHENIX (Adams et al, 2010) and Coot (Emsley et al, 2010).…”

Section: Peptide Synthesissupporting

confidence: 59%

“…Several structures of S100 proteins in complexes with their respective ligands have been published, including S100B in complex with a CapZ peptide (TRTK12; Charpentier et al, 2010), S100A11 in complex with the annexin A1 N-terminus (Ré ty et al, 2000) and S100A4 in complex with myosin IIA (Kiss et al, 2012). While these complexes generally have a quaternary structure similar to that of (p11) 2 (AnxA2) 2 , namely a peptide bound in each hydrophobic pocket of the activated S100 dimer (1:1 ratio of S100 protein:ligand), the structure of S100A4 in complex with a myosin IIA peptide was the first to reveal a asymmetric binding motif in which one peptide binds to the S100A4 dimer (1:2).…”

Section: Comparison With Other S100 Structuresmentioning

confidence: 99%

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Structure of a C-terminal AHNAK peptide in a 1:2:2 complex with S100A10 and an acetylated N-terminal peptide of annexin A2

Ozorowski

Milton

Luecke

2012

Acta Crystallogr D Biol Crystallogr

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AHNAK, a large 629 kDa protein, has been implicated in membrane repair, and the annexin A2–S100A10 heterotetramer [(p11)2(AnxA2)2)] has high affinity for several regions of its 1002‐amino‐acid C‐terminal domain. (p11)2(AnxA2)2 is often localized near the plasma membrane, and this C2‐symmetric platform is proposed to be involved in the bridging of membrane vesicles and trafficking of proteins to the plasma membrane. All three proteins co‐localize at the intracellular face of the plasma membrane in a Ca2+‐dependent manner. The binding of AHNAK to (p11)2(AnxA2)2 has been studied previously, and a minimal binding motif has been mapped to a 20‐amino‐acid peptide corresponding to residues 5654–5673 of the AHNAK C‐terminal domain. Here, the 2.5 Å resolution crystal structure of this 20‐amino‐acid peptide of AHNAK bound to the AnxA2–S100A10 heterotetramer (1:2:2 symmetry) is presented, which confirms the asymmetric arrangement first described by Rezvanpour and coworkers and explains why the binding motif has high affinity for (p11)2(AnxA2)2. Binding of AHNAK to the surface of (p11)2(AnxA2)2 is governed by several hydrophobic interactions between side chains of AHNAK and pockets on S100A10. The pockets are large enough to accommodate a variety of hydrophobic side chains, allowing the consensus sequence to be more general. Additionally, the various hydrogen bonds formed between the AHNAK peptide and (p11)2(AnxA2)2 most often involve backbone atoms of AHNAK; as a result, the side chains, particularly those that point away from S100A10/AnxA2 towards the solvent, are largely interchangeable. While the structure‐based consensus sequence allows interactions with various stretches of the AHNAK C‐terminal domain, comparison with other S100 structures reveals that the sequence has been optimized for binding to S100A10. This model adds new insight to the understanding of the specific interactions that occur in this membrane‐repair scaffold.

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Section: Peptide Synthesissupporting

confidence: 59%

Section: Comparison With Other S100 Structuresmentioning

confidence: 99%

Structure of a C-terminal AHNAK peptide in a 1:2:2 complex with S100A10 and an acetylated N-terminal peptide of annexin A2

Ozorowski

Milton

Luecke

2012

Acta Crystallogr D Biol Crystallogr

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“…The S100A8͞A9 heterodimer acts extracellularly as a chemotactic molecule in inflammation (85). S100A10 and S100A11 bind to distinct annexin proteins and regulate annexin trafficking to cell membranes (48,49). S100A12 is expressed in phagocytes, where it regulates secretion of proinflammatory mediators (50).…”

Section: Functional Diversity Of Ncs and S100 Proteinsmentioning

confidence: 99%

Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality

Ikura

Ames

2006

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

239

202

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Calcium signaling pathways control a variety of cellular events such as gene transcription, protein phosphorylation, nucleotide metabolism, and ion transport. These pathways often involve a large number of calcium-binding proteins collectively known as the calmodulin or EF-hand protein superfamily. Many EF-hand proteins undergo a large conformational change upon binding to Ca 2؉ and target proteins. All members of the superfamily share marked sequence homology and similar structural features required to sense Ca 2؉ . Despite such structural similarities, the functional diversity of EF-hand calcium-binding proteins is extraordinary. Calmodulin itself can bind >300 different proteins, and the many members of the neuronal calcium sensor and S100 protein families collectively recognize a largely different set of target proteins. Recent biochemical and structural studies of many different EF-hand proteins highlight remarkable similarities and variations in conformational responses to the common ligand Ca 2؉ and their respective cellular targets. In this review, we examine the essence of molecular recognition activities and the mechanisms by which calmodulin superfamily proteins control a wide variety of Ca 2؉ signaling processes.

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“…While the amphiphilic ␣-helices in annexins are specific, since each helix binds only one type of S100 protein (31), the C-terminal fragment of CacyBP/SIP binds several S100 proteins (present work). To reveal the mechanism underlying the difference in specificity of CacyBP/SIP and annexins toward S100 proteins, structural studies of CacyBP/SIP-S100 complexes should be performed and the data compared with that obtained for annexin-S100 protein complexes (31,32).…”

Section: Identification Of S100b As a Cacybp/sip Ligand In Thementioning

confidence: 99%

CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family

Filipek¹,

Jastrzębska²,

Nowotny³

et al. 2002

Journal of Biological Chemistry

135

107

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Recently, a human ortholog of mouse calcyclin (S100A6)-binding protein (CacyBP) called SIP (Siah-1-interacting protein) was shown to be a component of a novel ubiquitinylation pathway regulating ␤-catenin degradation (Matsuzawa, S., and Reed, J. C. (2001) Mol. Cell 7, 915-926). In murine brain, CacyBP/SIP is expressed at a high level, but S100A6 is expressed at a very low level. Consequently we carried out experiments to determine if CacyBP/SIP binds to other S100 proteins in this tissue. Using CacyBP/SIP affinity chromatography, we found that S100B from the brain extract binds to CacyBP/SIP in a Ca 2؉ -dependent manner. Using a nitrocellulose overlay assay with 125 I-CacyBP/SIP and CacyBP/SIP affinity chromatography, we found that this protein binds purified S100A1, S100A6, S100A12, S100B, and S100P but not S100A4, calbindin D 9k , parvalbumin, and calmodulin.

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Structural basis of the Ca2+-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I

Cited by 185 publications

References 59 publications

Structure of a C-terminal AHNAK peptide in a 1:2:2 complex with S100A10 and an acetylated N-terminal peptide of annexin A2

Structure of a C-terminal AHNAK peptide in a 1:2:2 complex with S100A10 and an acetylated N-terminal peptide of annexin A2

Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality

CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family

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