High impact information on NCU04173.1

• These genes encode novel proteins as well as proteins which 1) regulate the actin or microtubule cytoskeleton, 2) are kinases or components of signal transduction pathways, 3) are part of the secretory pathway, or 4) have functions in cell wall formation or membrane biosynthesis [1].
• Null mutants of the neurospora actin-related protein 1 pointed-end complex show distinct phenotypes [2].
• The ability to assemble cytoplasmic microtubules and actin is maintained in ro-2 mutants, although subapical actin patches are more prominent [3].
• In contrast, the accumulation of mRNAs encoding beta-tubulin, actin, or glyceraldehyde-3-phosphate dehydrogenase was not appreciably altered by either the presence of a hypovirulence-associated virus or treatment with cycloheximide [4].
• Actin has a pivotal function in hyphal morphogenesis in filamentous fungi, but it is not certain whether its function is equivalent to that of a morphogen, or if it is simply part of a mechanism that executes orders given by another regulatory entity [5].

Biological context of NCU04173.1

• Similar kinetics were observed with actin synthesis and tubulin mRNA [6].
• The actin-VDAC interaction might be a mechanism by which actin regulates energy metabolism [7].
• Our results suggest that by altering the conformation binding site of actin to p47, calmodulin could play a regulatory role in the polarized hyphal growth of N. crassa [8].

Anatomical context of NCU04173.1

• We conclude that the tip-high Ca2+ gradient is generated internally by Ca2+ sequestration into endoplasmic reticulum behind the tip and Ca2+ release via an IP3 receptor from tip-localized vesicles whose location is maintained by the actin cytoskeleton [9].
• Inhibitors of microtubules, but not of actin microfilaments, caused hyphae to lose their growth directionality-providing support for the idea that Spitzenkörper trajectory is determined internally by a growing scaffolding of cytoplasmic microtubules [10].
• Here we present evidence that actin can modulate the gating process of Neurospora crassa VDAC reconstituted into membranes made with phosphatidylcholine [7].
• This protein was identified as actin on immunoblots when an anti-actin monoclonal antibody raised against chicken gizzards was used as a probe [11].
• Apical actin could be involved in hyphal morphogenesis, organelle motility and maintenance of polarity [11].

Associations of NCU04173.1 with chemical compounds

• Conversely, disruption of actin with latrunculin B dissipated tip-localized Ca2+ [9].
• By cell fractionation and immunocytochemistry we show that proteins with characteristics of actin, spectrin, and integrin are associated in a MS-like manner with the PM of Neurospora crassa hyphae [12].
• The distribution of actin in hyphae was examined by FITC-phalloidin staining of formaldehyde fixed hyphae [11].

Analytical, diagnostic and therapeutic context of NCU04173.1

• To decode the internal mechanisms which generate and maintain the tip-high Ca2+ gradient we first identified calcium regulators which affect hyphal growth and morphology, then determined how they modify cytosolic [Ca2+] and the actin cytoskeleton using fluorescent dyes and confocal microscopy [9].
• Used as immunofluorescence probes, they allowed localization of actin in the sequential gametophytic stages of the mould [13].
• After two-dimensional gel electrophoresis three actin isoforms were detected [11].
• Highly specific polyclonal antibodies against actin from Allomyces arbuscula were produced in rabbits, immunopurified by immunoblotting and specified with actin isolated from Neurospora crassa and mouse skeletal muscle [13].
• Direct measurement of VDAC-actin interaction by surface plasmon resonance [14].

References