Disease relevance of ECM1

• Two strains of Candida albicans and one strain of Candida tropicalis bound avidly to exposed ECM, but Pseudomonas aeruginosa did not [1].
• The adherence of Candida albicans to extracellular matrix proteins may be a critical step in the pathogenesis of candidiasis [2].
• It was also detected in areas of fibrosis and necrosis, as well as disperse in amorphous extracellular matrix, mostly in resistant mice [3].

High impact information on ECM1

• Our previous work demonstrated that Mmp1 is required for growth of the tracheal system, and we suggested that the mutant phenotype resulted from aberrant persistence of cell adhesion to the extracellular matrix [4].
• Remarkably, cellular processes other than extracellular matrix biosynthesis and the formation of protein storage vacuoles appear unaffected in knf embryos [5].
• The dynamic localization of Wsc1p, a sensor of the extracellular wall in yeast, resembles polarized distribution of certain extracellular matrix-sensing integrins through endocytic recycling [6].
• The crystal structure of an Ecm1-sinefungin binary complex reveals sinefungin-specific polar contacts with main-chain and side-chain atoms that can explain the 3-fold higher affinity of Ecm1 for sinefungin versus AdoMet or S-adenosylhomocysteine (AdoHcy) [7].
• We purified 45 Ecm1 mutant proteins and assayed them for methylation of GpppA in vitro [7].

Biological context of ECM1

• This domestication is accompanied by loss of the ECM and by extensive changes in gene expression as detected by DNA microarrays [8].
• However, treatment of endothelium with forskolin, which induces cell shape changes without exposure of the ECM, did not cause an increase in adherence [1].
• Defects in assembly of the extracellular matrix are responsible for altered morphogenesis of a Candida albicans phr1 mutant [9].
• The transforming growth factors beta control a diversity of biological processes including cellular proliferation, differentiation, apoptosis, and extracellular matrix production, and are critical effectors of embryonic patterning and development, including that of the orofacial region [10].
• Variations of the electrical conductivity of the intra- and extracellular matrix caused by ions and solutes transfer across the membrane were shown to be involved in the observed heating [11].

Anatomical context of ECM1

• In the yeast Saccharomyces cerevisiae, environmental stress conditions that damage the cell wall lead to activation of the so-called "compensatory mechanism," aimed at preserving cell integrity through a remodeling of this extracellular matrix [12].
• Integrin binding to extracellular matrix proteins induces formation of signaling complexes at focal adhesions [13].
• The Arabidopsis wall-associated receptor kinase, Wak1, is a member of the Wak family (Wak1-5) that links the plasma membrane to the extracellular matrix [14].
• ATP, which is present in the extracellular matrix of multicellular organisms and in the extracellular fluid of unicellular organisms, has been shown to function as a signaling molecule in animals [15].
• We have investigated the interaction between Candida albicans and entactin, a recently characterized glycoprotein present in the extracellular matrix, especially in the basement membrane [16].

Associations of ECM1 with chemical compounds

• Consistent with these results, we found that the subcellular localization of Cas and 14-3-3 is also regulated by integrin ligand binding and that the two proteins display a significant co-localization during cell attachment to the extracellular matrix [17].
• The natural product antibiotic sinefungin is an AdoMet analog that inhibits Ecm1 with modest potency [7].
• SDS extracts that interacted with all the extracellular matrix protein were tested; their molecular masses were 19 and 32 kDa [18].
• Bovine vascular endothelial cells treated with EDTA, urea, or thrombin underwent a marked, reversible contraction resulting in exposure of the subendothelial extracellular matrix (ECM) [1].
• Furthermore, in these experimental conditions, the effect of sub-inhibitory concentrations of antifungals on adherence was dependent on the tested antifungal and the adherence surface: amphotericin B inhibited adherence to polystyrene and fibrinogen, but improved adherence to extracellular matrix [19].

Other interactions of ECM1

• A null mutation in KTR2 leads to partial resistance to killer toxin and hints that KTR2, which encodes a putative mannosyltransferase, is involved in extracellular matrix assembly [20].
• Because Bud10p contains a large extracellular domain, it is possible that Bud10p functions in a manner analogous to an extracellular matrix receptor [21].

Analytical, diagnostic and therapeutic context of ECM1

• Environmental scanning electron microscopy shows that the cells within wild fluffy colonies are connected by extracellular matrix (ECM) material [8].
• In indirect immunofluorescence assays with polyclonal antibodies directed towards the ECM proteins, both hyphae and yeast cells of S. schenckii exhibited the ability to bind laminin and fibronectin [22].
• Immunofluorescence microscopy and flow cytometry demonstrated that all three ECM proteins tested were able to bind to the surface of P. brasiliensis yeast cells [23].

References