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Structural insights into calmodulin-regulated L-selectin ectodomain shedding.

Gifford JL, Ishida H, Vogel HJ
J Biol Chem 287 26513-27 (2012)
Cited: 20 times
EuropePMC logo PMID: 22711531

Abstract

The L-selectin glycoprotein receptor mediates the initial steps of leukocyte migration into secondary lymphoid organs and sites of inflammation. Following cell activation through the engagement of G-protein-coupled receptors or immunoreceptors, the extracellular domains of L-selectin are rapidly shed, a process negatively controlled via the binding of the ubiquitous eukaryotic calcium-binding protein calmodulin to the cytoplasmic tail of L-selectin. Here we present the solution structure of calcium-calmodulin bound to a peptide encompassing the cytoplasmic tail and part of the transmembrane domain of L-selectin. The structure and accompanying biophysical study highlight the importance of both calcium and the transmembrane segment of L-selectin in the interaction between these two proteins, suggesting that by binding this region, calmodulin regulates in an "inside-out" fashion the ectodomain shedding of the receptor. Our structure provides the first molecular insight into the emerging new role for calmodulin as a transmembrane signaling partner.

Articles - 2lgf mentioned but not cited (5)

  1. Structural insights into calmodulin-regulated L-selectin ectodomain shedding. Gifford JL, Ishida H, Vogel HJ. J Biol Chem 287 26513-26527 (2012)
  2. Calmodulin adopts an extended conformation when interacting with L-selectin in membranes. Deng W, Putkey JA, Li R. PLoS One 8 e62861 (2013)
  3. Modeling of RAS complexes supports roles in cancer for less studied partners. Engin HB, Carlin D, Pratt D, Carter H. BMC Biophys 10 5 (2017)
  4. The cytoplasmic tail of L-selectin interacts with the adaptor-protein complex AP-1 subunit μ1A via a novel basic binding motif. Dib K, Tikhonova IG, Ivetic A, Schu P. J Biol Chem 292 6703-6714 (2017)
  5. Coarse-Grained Modeling and Molecular Dynamics Simulations of Ca2+-Calmodulin. Nde J, Zhang P, Ezerski JC, Lu W, Knapp K, Wolynes PG, Cheung MS. Front Mol Biosci 8 661322 (2021)


Reviews citing this publication (5)

  1. Structural diversity of calmodulin binding to its target sites. Tidow H, Nissen P. FEBS J 280 5551-5565 (2013)
  2. L-selectin: A Major Regulator of Leukocyte Adhesion, Migration and Signaling. Ivetic A, Hoskins Green HL, Hart SJ. Front Immunol 10 1068 (2019)
  3. A head-to-tail view of L-selectin and its impact on neutrophil behaviour. Ivetic A. Cell Tissue Res 371 437-453 (2018)
  4. Gap junction regulation by calmodulin. Zou J, Salarian M, Chen Y, Veenstra R, Louis CF, Yang JJ. FEBS Lett 588 1430-1438 (2014)
  5. Juxtamembrane contribution to transmembrane signaling. Deng W, Li R. Biopolymers 104 317-322 (2015)

Articles citing this publication (10)

  1. A disintegrin and metalloprotease (ADAM) 10 and ADAM17 are major sheddases of T cell immunoglobulin and mucin domain 3 (Tim-3). Möller-Hackbarth K, Dewitz C, Schweigert O, Trad A, Garbers C, Rose-John S, Scheller J. J Biol Chem 288 34529-34544 (2013)
  2. The Structural Basis of the Farnesylated and Methylated KRas4B Interaction with Calmodulin. Jang H, Banerjee A, Marcus K, Makowski L, Mattos C, Gaponenko V, Nussinov R. Structure 27 1647-1659.e4 (2019)
  3. Molecular Dynamics of the Association of L-Selectin and FERM Regulated by PIP2. Sun F, Schroer CFE, Xu L, Yin H, Marrink SJ, Luo SZ. Biophys J 114 1858-1868 (2018)
  4. Comparing the calcium binding abilities of two soybean calmodulins: towards understanding the divergent nature of plant calmodulins. Gifford JL, Jamshidiha M, Mo J, Ishida H, Vogel HJ. Plant Cell 25 4512-4524 (2013)
  5. Structural characterization of the interaction of human lactoferrin with calmodulin. Gifford JL, Ishida H, Vogel HJ. PLoS One 7 e51026 (2012)
  6. Structure and function insights garnered from in silico modeling of the thrombospondin type-1 domain-containing 7A antigen. Stoddard SV, Welsh CL, Palopoli MM, Stoddard SD, Aramandla MP, Patel RM, Ma H, Beck LH. Proteins 87 136-145 (2019)
  7. T-cell immunoglobulin and mucin domain 2 (TIM-2) is a target of ADAM10-mediated ectodomain shedding. Dewitz C, Möller-Hackbarth K, Schweigert O, Reiss K, Chalaris A, Scheller J, Rose-John S. FEBS J 281 157-174 (2014)
  8. Thrombin-derived host defence peptide modulates neutrophil rolling and migration in vitro and functional response in vivo. Lim CH, Puthia M, Butrym M, Tay HM, Lee MZY, Hou HW, Schmidtchen A. Sci Rep 7 11201 (2017)
  9. Over-expression of a human CD62L ecto-domain and a potential role of RNA pseudoknot structures in recombinant protein expression. Spencer M, Max N, Ireland J, Zou Z, Wang R, Sun P. Protein Expr Purif 140 65-73 (2017)
  10. The Recognition of Calmodulin to the Target Sequence of Calcineurin-A Novel Binding Mode. Chyan CL, Irene D, Lin SM. Molecules 22 E1584 (2017)


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