Emerson F et al. (2020) Elife "A memory of longevity."

Lee SS, Li CL, Emerson F

[Elife, 2020]

Worms with increased levels of the epigenetic mark H3K9me2 have a longer lifespan that can be passed down to future generations.

Harker AJ et al. (2019) Mol Biol Cell "Ena/VASP processive elongation is modulated by avidity on actin filaments bundled by the filopodia crosslinker fascin."

Bidone TC, Harker AJ, Katkar HH, Applewhite DA, Kovar DR, Voth GA, Aydin F

[Mol Biol Cell, 2019]

Ena/VASP tetramers are processive actin elongation factors that localize to diverse F-actin networks composed of filaments bundled by different crosslinking proteins, such as filopodia (fascin), lamellipodia (fimbrin), and stress fibers (-actinin). Previously, we found that Ena takes 3-fold longer processive runs on trailing barbed ends of fascin-bundled F-actin. Here, we used single-molecule TIRFM and developed a kinetic model to further dissect Ena/VASP's processive mechanism on bundled filaments. We discovered that Ena's enhanced processivity on trailing barbed ends is specific to fascin bundles, with no enhancement on fimbrin or -actinin bundles. Notably, Ena/VASP's processive run length increases with the number of both fascin-bundled filaments and Ena 'arms', revealing avidity facilitates enhanced processivity. Consistently, Ena tetramers form more filopodia than mutant dimer and trimers in Drosophila culture cells. Moreover, enhanced processivity on trailing barbed ends of fascin-bundled filaments is an evolutionarily conserved property of Ena/VASP homologs, including human VASP and C. elegans UNC-34. These results demonstrate that Ena tetramers are tailored for enhanced processivity on fascin bundles and avidity of multiple arms associating with multiple filaments is critical for this process. Furthermore, we discovered a novel regulatory process whereby bundle size and bundling protein specificity control activities of a processive assembly factor. Movie S1 Movie S1 EnaL processivity on fascin bundles (corresponds to Figure 1, C, D, I, and K). Spontaneous assembly of 1.5 M Mg-ATP-actin (15% Oregon green-actin) with 15 pM SNAP(549)-EnaL (red) and unlabeled 130 nM human fascin visualized by two-color TIRFM. White arrowheads mark free slow-growing barbed ends, and yellow arrowheads mark fast growing barbed ends associated with EnaL. Time interval between frames is 1 s. Movie S2 Movie S2 UNC-34 processivity on fascin bundles (corresponds to Figure 2, F and G). Spontaneous assembly of 1.5 M Mg-ATP-actin (15% Oregon green-actin) with 18 pM SNAP(549)-UNC-34 (red) and unlabeled 130 nM human fascin visualized by two-color TIRFM. White arrowheads mark free slow-growing barbed ends, and yellow arrowheads mark fast growing barbed ends associated with UNC-34. Time interval between frames is 0.5 s. Movie S3 Movie S3 EnaLDimer processivity on fascin bundles (corresponds to Figure 3, B, C, and E). Spontaneous assembly of 1.5 M Mg-ATP-actin (15% Alexa488-actin) with 50 pM MBP-SNAP(549)-EnaLCC-GCN4 (red) and unlabeled 130 nM human fascin visualized by two-color TIRFM. White arrowheads mark free slow-growing barbed ends, and yellow arrowheads mark fast growing barbed ends associated with EnaLDimer. Time interval between frames is 0.5 s.

Wu Y et al. (2017) Curr Top Dev Biol "Regulation of Cell Polarity by PAR-1/MARK Kinase."

Wu Y, Griffin EE

[Curr Top Dev Biol, 2017]

PAR-1/MARK kinases are conserved serine/threonine kinases that are essential regulators of cell polarity. PAR-1/MARK kinases localize and function in opposition to the anterior PAR proteins to control the asymmetric distribution of factors in a wide variety polarized cells. In this review, we discuss the mechanisms that control the localization and activity of PAR-1/MARK kinases, including their antagonistic interactions with the anterior PAR proteins. We focus on the role PAR-1 plays in the asymmetric division of the Caenorhabditis elegans zygote, in the establishment of the anterior/posterior axis in the Drosophila oocyte and in the control of microtubule dynamics in mammalian neurons. In addition to conserved aspects of PAR-1 biology, we highlight the unique ways in which PAR-1 acts in these distinct cell types to orchestrate their polarization. Finally, we review the connections between disruptions in PAR-1/MARK function and Alzheimer's disease and cancer.

Benecke M et al. (1994) Worm Breeder's Gazette "DNA Fingerprinting in C. elegans - An Approach."

Epplen JT, Schierenberg E, Benecke M

[Worm Breeder's Gazette, 1994]

DNA fingerprinting in C. elegans - an approach Mark Beneckea, Jorg T. Epplenb and Einhard Schierenberga a Zoologisches Institut der Univeritat, 50923 Koln, Germany b Ruhr-Universitat, Ab1. fur Molekulare Humangenetik, 44780 Bochum, Germany

Butkevich E et al. (2016) Sci Rep "Phosphorylation of FEZ1 by Microtubule Affinity Regulating Kinases regulates its function in presynaptic protein trafficking."

Grosche J, Erck C, Urlaub H, Nikolov M, Klopfenstein DR, Butkevich E, Chua JJ, Hartig W, Schmidt CF

[Sci Rep, 2016]

Adapters bind motor proteins to cargoes and therefore play essential roles in Kinesin-1 mediated intracellular transport. The regulatory mechanisms governing adapter functions and the spectrum of cargoes recognized by individual adapters remain poorly defined. Here, we show that cargoes transported by the Kinesin-1 adapter FEZ1 are enriched for presynaptic components and identify that specific phosphorylation of FEZ1 at its serine 58 regulatory site is mediated by microtubule affinity-regulating kinases (MARK/PAR-1). Loss of MARK/PAR-1 impairs axonal transport, with adapter and cargo abnormally co-aggregating in neuronal cell bodies and axons. Presynaptic specializations are markedly reduced and distorted in FEZ1 and MARK/PAR-1 mutants. Strikingly, abnormal co-aggregates of unphosphorylated FEZ1, Kinesin-1 and its putative cargoes are present in brains of transgenic mice modelling aspects of Alzheimer's disease, a neurodegenerative disorder exhibiting impaired axonal transport and altered MARK activity. Our findings suggest that perturbed FEZ1-mediated synaptic delivery of proteins arising from abnormal signalling potentially contributes to the process of neurodegeneration.

Blumenthal TE et al. (1993) Worm Breeder's Gazette "The C. elegans Cleavage and Polyadenylation Signal"

Fields CA, White O, Blumenthal TE

[Worm Breeder's Gazette, 1993]

THE C. ELEGANS CLEAVAGE AND POLYADENYLATION SlGNAL Tom Blumenthal, Department of Biology, Indiana University. Bloomington, IN 47405; Owen White and Chris Fields, Institute For Genomic Research, Gaithersburg, MD, 20878

Vanfleteren JR (1976) Nematologica "The nature of a nematode growth factor. III. Growth and maturation of C. briggsae on protein-haemin co-precipitates."

Vanfleteren JR

[Nematologica, 1976]

The growth promoting activity of protein-haemin co-precipitates from ferritin, apoferritin, transferrin, bovine serum albumin, conalbumin and egg white on maturation and reproduction of C. briggsae has been evaluated. Ferritin, apoferritin and transferrin were found to be biologically highly active in the presence of haemin. Bovine serum albumin, conalbumin and egg white were slightly active. Maturation and reproduction of C. briggsae on the coagulates from bovine serum albumin and egg white were nearly independent of the dose administered, probably because the limited availability of haemin from these coagulates permits but slow growth, even in the presence of abundant proteinaceous material. Bovine serum albumin, egg white and conalbumin failed to support continuous growth of C. briggsae. It is supposed that the limited availability of haemin from these coagulates inhibits normal maturation and reproduction of the F1 progeny. These experiments clearly demonstrate the requirement for particulate haem. The requirement for

Hobert O et al. (1999) Worm Breeder's Gazette "Neuroanatomy-- A second look with GFP reporters and some comments"

Hobert O, Hall DH

[Worm Breeder's Gazette, 1999]

For everyone who deals with the characterization of expression patterns in the nervous system, the truly impressive paper of White et al., 1986 ("Mind of the Worm") serves as the ultimate source of knowledge. While the largely invariant neural cell body positions described by Sulston et al. are an essential tool in the identification of neurons, the axon morphologies described by White et al. greatly facilitate the identification of a given neuron.

Skourti-Stathaki K et al. (2013) Mol Cell "Histone 3 s10 phosphorylation: "caught in the R loop!"."

Skourti-Stathaki K, Proudfoot NJ

[Mol Cell, 2013]

In this issue of Molecular Cell, Castellano-Pozo etal. (2013) describe a connection between R loop structures and histone 3 S10 phosphorylation (H3S10P), a mark of chromatin compaction. Their results constitute asignificant advance in our understanding of the role of R loops in genomic instability.

Bohdanowicz M et al. (2010) Curr Biol "Vesicular traffic: a Rab SANDwich."

Bohdanowicz M, Grinstein S

[Curr Biol, 2010]

The small GTPases Rab5 and Rab7 mark temporally distinct but sequentially connected stages in phagosome maturation, but the mechanism underlying the transition between these stages has been unclear. Recent studies in Caenorhabditis elegans have now uncovered a new protein complex that connects Rab5 to Rab7.