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The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain.

Sonnenberg A, Rojas AM, de Pereda JM
J Mol Biol 368 1379-91 (2007)
Cited: 35 times
EuropePMC logo PMID: 17397861

Abstract

Plectin is a large and versatile cytoskeletal linker and member of the plakin protein family. Plakins share a conserved region called the plakin domain located near their N terminus. We have determined the crystal structure of an N-terminal fragment of the plakin domain of plectin to 2.05 A resolution. This region is adjacent to the actin-binding domain and is required for efficient binding to the integrin alpha6beta4 in hemidesmosomes. The structure is formed by two spectrin repeats connected by an alpha-helix that spans these two repeats. While the first repeat is very similar to other known structures, the second repeat is structurally different with a hydrophobic core, narrower than that in canonical spectrin repeats. Sequence analysis of the plakin domain revealed the presence of up to nine consecutive spectrin repeats organized in an array of tandem modules, and a Src-homology 3 domain inserted in the central spectrin repeat. The structure of the plakin domain is reminiscent of the modular organization of members of the spectrin family. The architecture of the plakin domain suggests that it forms an elongated and flexible structure, and provides a novel molecular explanation for the contribution of plectin and other plakins to the elasticity and stability of tissues subjected to mechanical stress, such as the skin and striated muscle.

Reviews - 2odu mentioned but not cited (1)

  1. Advances and perspectives of the architecture of hemidesmosomes: lessons from structural biology. de Pereda JM, Ortega E, Alonso-García N, Gómez-Hernández M, Sonnenberg A. Cell Adh Migr 3 361-364 (2009)

Articles - 2odu mentioned but not cited (3)

  1. Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein. Subramanian R, Wilson-Kubalek EM, Arthur CP, Bick MJ, Campbell EA, Darst SA, Milligan RA, Kapoor TM. Cell 142 433-443 (2010)
  2. Crystal structure of a rigid four-spectrin-repeat fragment of the human desmoplakin plakin domain. Choi HJ, Weis WI. J Mol Biol 409 800-812 (2011)
  3. Whole Exome Sequencing Confirms Molecular Diagnostics of Three Pakhtun Families With Autosomal Recessive Epidermolysis Bullosa. Fozia F, Nazli R, Bibi N, Khan SA, Muhammad N, Shakeeb N, Khan S, Jelani M, Wasif N. Front Pediatr 9 727288 (2021)


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  1. Introducing intermediate filaments: from discovery to disease. Eriksson JE, Dechat T, Grin B, Helfand B, Mendez M, Pallari HM, Goldman RD. J Clin Invest 119 1763-1771 (2009)
  2. Plakins in development and disease. Sonnenberg A, Liem RK. Exp Cell Res 313 2189-2203 (2007)
  3. Spectraplakins: master orchestrators of cytoskeletal dynamics. Suozzi KC, Wu X, Fuchs E. J Cell Biol 197 465-475 (2012)
  4. Functions of the intermediate filament cytoskeleton in the eye lens. Song S, Landsbury A, Dahm R, Liu Y, Zhang Q, Quinlan RA. J Clin Invest 119 1837-1848 (2009)
  5. Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve. Castañón MJ, Walko G, Winter L, Wiche G. Histochem Cell Biol 140 33-53 (2013)
  6. Mechanistic basis of desmosome-targeted diseases. Al-Jassar C, Bikker H, Overduin M, Chidgey M. J Mol Biol 425 4006-4022 (2013)
  7. The cytoskeleton and neurite initiation. Flynn KC. Bioarchitecture 3 86-109 (2013)
  8. Cytoskeletal Integrators: The Spectrin Superfamily. Liem RK. Cold Spring Harb Perspect Biol 8 a018259 (2016)
  9. One gene but different proteins and diseases: the complexity of dystonin and bullous pemphigoid antigen 1. Künzli K, Favre B, Chofflon M, Borradori L. Exp Dermatol 25 10-16 (2016)
  10. Isoforms, structures, and functions of versatile spectraplakin MACF1. Hu L, Su P, Li R, Yin C, Zhang Y, Shang P, Yang T, Qian A. BMB Rep 49 37-44 (2016)
  11. Spectraplakin family proteins - cytoskeletal crosslinkers with versatile roles. Zhang J, Yue J, Wu X. J Cell Sci 130 2447-2457 (2017)
  12. Epidermolysis bullosa simplex with muscular dystrophy. Chiavérini C, Charlesworth A, Meneguzzi G, Lacour JP, Ortonne JP. Dermatol Clin 28 245-55, viii (2010)
  13. Impact of keratin intermediate filaments on insulin-mediated glucose metabolism regulation in the liver and disease association. Roux A, Gilbert S, Loranger A, Marceau N. FASEB J 30 491-502 (2016)
  14. BPAG1 in muscles: Structure and function in skeletal, cardiac and smooth muscle. Horie M, Yoshioka N, Takebayashi H. Semin Cell Dev Biol 69 26-33 (2017)
  15. The spectraplakins of Caenorhabditis elegans: Cytoskeletal crosslinkers and beyond. Fu R, Jiang X, Huang Z, Zhang H, Zhang H. Semin Cell Dev Biol 69 58-68 (2017)
  16. Role of microtubule actin crosslinking factor 1 (MACF1) in bipolar disorder pathophysiology and potential in lithium therapeutic mechanism. Salem D, Fecek RJ. Transl Psychiatry 13 221 (2023)

Articles citing this publication (15)

  1. Structures of the spectrin-ankyrin interaction binding domains. Ipsaro JJ, Huang L, Mondragón A. Blood 113 5385-5393 (2009)
  2. Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes. de Pereda JM, Lillo MP, Sonnenberg A. EMBO J 28 1180-1190 (2009)
  3. The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties. Stabach PR, Simonović I, Ranieri MA, Aboodi MS, Steitz TA, Simonović M, Morrow JS. Blood 113 5377-5384 (2009)
  4. Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex. Ipsaro JJ, Harper SL, Messick TE, Marmorstein R, Mondragón A, Speicher DW. Blood 115 4843-4852 (2010)
  5. Letter PLEC1 mutations underlie adult-onset dilated cardiomyopathy in epidermolysis bullosa simplex with muscular dystrophy. Bolling MC, Pas HH, de Visser M, Aronica E, Pfendner EG, van den Berg MP, Diercks GF, Suurmeijer AJ, Jonkman MF. J Invest Dermatol 130 1178-1181 (2010)
  6. Phosphorylation of threonine 1736 in the C-terminal tail of integrin β4 contributes to hemidesmosome disassembly. Frijns E, Kuikman I, Litjens S, Raspe M, Jalink K, Ports M, Wilhelmsen K, Sonnenberg A. Mol Biol Cell 23 1475-1485 (2012)
  7. Plectin contributes to mechanical properties of living cells. Na S, Chowdhury F, Tay B, Ouyang M, Gregor M, Wang Y, Wiche G, Wang N. Am J Physiol Cell Physiol 296 C868-77 (2009)
  8. The structure of the plakin domain of plectin reveals a non-canonical SH3 domain interacting with its fourth spectrin repeat. Ortega E, Buey RM, Sonnenberg A, de Pereda JM. J Biol Chem 286 12429-12438 (2011)
  9. The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape. Ortega E, Manso JA, Buey RM, Carballido AM, Carabias A, Sonnenberg A, de Pereda JM. J Biol Chem 291 18643-18662 (2016)
  10. BPAG1a and b associate with EB1 and EB3 and modulate vesicular transport, Golgi apparatus structure, and cell migration in C2.7 myoblasts. Poliakova K, Adebola A, Leung CL, Favre B, Liem RK, Schepens I, Borradori L. PLoS One 9 e107535 (2014)
  11. The crystal structures of dystrophin and utrophin spectrin repeats: implications for domain boundaries. Muthu M, Richardson KA, Sutherland-Smith AJ. PLoS One 7 e40066 (2012)
  12. BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin. Steiner-Champliaud MF, Schneider Y, Favre B, Paulhe F, Praetzel-Wunder S, Faulkner G, Konieczny P, Raith M, Wiche G, Adebola A, Liem RK, Langbein L, Sonnenberg A, Fontao L, Borradori L. Exp Cell Res 316 297-313 (2010)
  13. Hinged plakin domains provide specialized degrees of articulation in envoplakin, periplakin and desmoplakin. Al-Jassar C, Bernadό P, Chidgey M, Overduin M. PLoS One 8 e69767 (2013)
  14. Ase1 domains dynamically slow anaphase spindle elongation and recruit Bim1 to the midzone. Thomas EC, Ismael A, Moore JK. Mol Biol Cell 31 2733-2747 (2020)
  15. Haemostatic role of intermediate filaments in adhered platelets: importance of the membranous system stability. Cerecedo D, Martínez-Vieyra I, Mondragón R, Mondragón M, González S, Galván IJ. J Cell Biochem 114 2050-2060 (2013)


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