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The Triple Helix of Collagens – an Ancient Protein Structure That Enabled Animal Multicellularity and Tissue Evolution Aaron L

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The Triple Helix of Collagens – an Ancient Protein Structure That Enabled Animal Multicellularity and Tissue Evolution Aaron L © 2018. Published by The Company of Biologists Ltd | Journal of Cell Science (2018) 131, jcs203950. doi:10.1242/jcs.203950 OPINION The triple helix of collagens – an ancient protein structure that enabled animal multicellularity and tissue evolution Aaron L. Fidler1,2,*, Sergei P. Boudko1,2,*, Antonis Rokas3 and Billy G. Hudson1,2,4,5,6,7,8,9,‡ ABSTRACT are derived from a total of 46 α-chains across the superfamily (Fig. 1) The cellular microenvironment, characterized by an extracellular (Ricard-Blum, 2011; Kadler et al., 2007; Ricard-Blum and Ruggiero, matrix (ECM), played an essential role in the transition from 2005). Invertebrates generally contain collagen IV, XV or XVIII, unicellularity to multicellularity in animals (metazoans), and in the some fibrillar collagens, as well as some fibril-associated collagens subsequent evolution of diverse animal tissues and organs. A major with interrupted triple helices (FACITs) (Fidler et al., 2014, 2017; ECM component are members of the collagen superfamily – Fahey and Degnan, 2010; Meyer and Moussian, 2009; Boot-Handford comprising 28 types in vertebrates – that exist in diverse and Tuckwell, 2003; Whittaker et al., 2006; Kadler et al., 2007). supramolecular assemblies ranging from networks to fibrils. Each Among these collagens, type IV is the evolutionarily most ancient, assembly is characterized by a hallmark feature, a protein structure based on recent studies of non-bilaterian animals (sponges, called a triple helix. A current gap in knowledge is understanding the ctenophores, placozoans and cnidarians) and unicellular groups mechanisms of how the triple helix encodes and utilizes information in (Fidler et al., 2017; Grau-Bove et al., 2017) (Fig. 1). building scaffolds on the outside of cells. Type IV collagen, recently Collagens are the most abundant protein in the human body revealed as the evolutionarily most ancient member of the collagen (Kadler et al., 2007; Shoulders and Raines, 2009). They occur as superfamily, serves as an archetype for a fresh view of fundamental diverse supramolecular assemblies, ranging from networks to fibrils, structural features of a triple helix that underlie the diversity of and broadly function in structural, mechanical and organizational biological activities of collagens. In this Opinion, we argue that the roles that define tissue architecture and influence cellular behavior triple helix is a protein structure of fundamental importance in building (Shoulders and Raines, 2009; Ricard-Blum, 2011; Ricard-Blum and the extracellular matrix, which enabled animal multicellularity and Ruggiero, 2005). Defects in collagens underlie the cause of almost 40 tissue evolution. human genetic diseases, affecting numerous organs and tissues in millions of people worldwide (summarized in Table 1). KEY WORDS: Cell biology, Collagen, Evolution, Extracellular matrix, Disease pathogenesis typically involves genetic alterations of the Multicellularity, Triple helix triple helix, a unique structure that is a hallmark feature common to all collagens. The triple helix bestows exceptional mechanical Introduction resistance to tensile forces and a capacity to bind a plethora of The extracellular matrix (ECM) played an essential role during the macromolecules. Yet, there is a gap in our current knowledge in transition from unicellular organisms to multicellular animals understanding the mechanisms of how a triple helix encodes and (metazoans). The ECM comprises a basement membrane (BM) utilizes information in building supramolecular assemblies on the that underlies epithelia cells, and an interstitial matrix (IM) that is outside of cells. Here, we present collagen IV, the most ancient of positioned between cells in the intercellular spaces and undergoes the collagen superfamily, and argue that it is ideally suited to serve continuous controlled remodeling (Hynes, 2012; Bonnans et al., as an archetype for investigating and describing core functions of a 2014; Nelson and Bissell, 2006; Inman et al., 2015). Yet, a major triple helix. gap in cell biology is to understand how cells generate and interact with the ECM (Sherwood, 2015; Jayadev and Sherwood, 2017). The triple helix – assembly and structural features that The collagen superfamily of proteins is a major component encode information of ECMs, which – in vertebrates – comprises 28 types (I–XXVIII) that The chemical structure of the triple helix was determined through the seminal work of structural biologists and chemists over the last century (see Box 1 in supplementary material). Its unique structure 1Department of Medicine, Division of Nephrology and Hypertension, Vanderbilt bestows upon collagens an exceptional mechanical resistance to University Medical Center, Nashville, TN, 37232, USA. 2Center for Matrix Biology, Vanderbilt University Medical Center, Nashville, TN, 37232, USA. 3Department of tensile forces and a plethora of organizing information for building Biological Sciences, Vanderbilt University Medical Center, Nashville, TN, 37232, an ECM (Fig. 2). The triple helix presents all residues, except USA. 4Department of Pathology, Microbiology, and Immunology, Vanderbilt glycine (Gly), on its surface, which is the most economical and University Medical Center, Nashville, TN, 37232, USA. 5Department of Medical Education and Administration, Vanderbilt University Medical Center, Nashville, TN, robust way to encode binding motifs of any protein structure. 37232, USA. 6Department of Cell and Developmental Biology, Vanderbilt University Moreover, the triple helix exhibits extensive post-translational Medical Center, Nashville, TN, 37232, USA. 7Department of Biochemistry, 8 modifications (PTMs), such as hydroxylation, glycosylation and Vanderbilt University Medical Center, Nashville, TN, 37232, USA. Vanderbilt- – – Ingram Cancer Center, Vanderbilt University Medical Center, Nashville, TN, 37232, phosphorylation, adding in tandem a secondary layer of USA. 9Vanderbilt Institute of Chemical Biology, Vanderbilt University Medical information in addition to its amino acid (aa) code (Yamauchi and Center, Nashville, TN, 37232, USA. *These authors contributed equally to this work Shiiba, 2008). These PTMs confer even more diversity with tissue- specific and disease-specific variations, even amongst identical ‡Author for correspondence ([email protected]) types of collagen (Pokidysheva et al., 2013). Furthermore, A.L.F., 0000-0002-2519-8864; A.R., 0000-0002-7248-6551; B.G.H., 0000-0002- additional collagen modifications are mediated by specific 5420-4100 extracellular enzymes, such as peroxidasin and lysyl oxidases-like Journal of Cell Science 1 OPINION Journal of Cell Science (2018) 131, jcs203950. doi:10.1242/jcs.203950 Unicellular Multicellular Collagen superfamily Choanoflagellates Cnidarians Vertebrates Fibrillar collagens Ministeria vibrans Ctenophores Sponges Insects Multiplexins (filastereans) XXV I, II, III, V, XI, XXVIII XXIV, XXVII FACITs Anchoring fibrils IX, XII, XIV, XVI, VII Loss of XIX, XX, XXI, XXII collagen IV variant Beaded filaments MACITs XIII, XVII XXIII, XXV VI Network-forming collagens Misc. XXVI, XXVIII >700 million years of evolution IV VIII, X LCA collagen IV variant TripleTi l helixh li Fig. 1. Collagen IV is the evolutionarily most ancient of the vertebrate collagen superfamily. The collagen superfamily has 28 members in vertebrates, each comprising three of 46 α-chains – the basis of the diverse suprastructures distributed across different tissues – invertebrates have less members. A hallmark feature of all collagens is the triple helix, which is characterized by three intertwined polypeptide chains. A collagen IV-like gene probably first appeared in the last common ancestor (LCA) to filastereans, choanoflagellates and animals. The phylogenetic distribution suggests that collagen IV played a critical role in the transition of unicellular organisms to multicellular animals. FACITs, fibril-associated collagens with interrupted triple helices; MACITs, membrane-associated collagens with interrupted triple helices; Misc., miscellaneous. proteins (LOXLs) for crosslinking, and Goodpasture antigen- Rich and Crick, 1955; Okuyama et al., 1981). Moreover, as these binding protein (COL4A3BP, hereafter referred to as GPBP) and three chains wind together forming a triple helix, each individual other extracellular kinases for phosphorylation (Bhave et al., 2012; left-handed chain adopts a right-handed superhelix. The unique role Añazco et al., 2016; Revert et al. 1995, Raya et al. 1999; Yalak and of the glycine residues in the packing of the collagen triple helix Olsen, 2015). Non-enzymatic modifications, such as glycation, explains the adverse effects of mutations at these positions, as any oxidation or chlorination, add even more complexity (Brown et al., other residue in place of glycine will distort its tight packing (Bella 2015). Together, these modifications may serve as regulatory et al., 1994). mechanisms on the outside of cells that may instruct cell behavior Three main changes are achieved upon the transition from a and influence tissue architecture and stability (Yalak and Olsen, single polyproline helix to a triple helix: (i) higher bending rigidity, 2015; Pedchenko et al., 2010). (ii) a less accessible chain backbone that is, thus, less prone to To fully appreciate the capacity and versatility of the triple helix, proteolysis and, (iii) the ability to essentially accept any aa in place one should consider the building blocks (polypeptide chains) of this of the proline residues at
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