Physiology and Biophysics

Seminars

Sep
25
Tue
2018
2018 Lamport Lecture – Richard Vallee @ HSB T-639
Sep 25 @ 4:00 pm – 5:00 pm
2018 Lamport Lecture

Cytoplasmic Dynein and Kinesins in Brain Development and Autophagy

Microtubule Motor Proteins Are Involved in a Wide Range of cellular activities.  Recent work in our lab has involved the role of the motor proteins in neuronal migration and neurogenesis in the developing brain.  We have worked out mechanisms by which cytoplasmic dynein, its regulators Nde1 and Ndel1, and LIS1  and the kinesin Kif1a contribute to these functions as well as brain developmental disease. We have also found a new role for the dynein adaptor protein RILP as a master regulator of mTOR-dependent autophagy in neurons. Richard Vallee Professor of Pathology & Cell Biology Columbia University time: 4:00pm location: HSB, T-639 host: Stanley C. Froehner
Oct
4
Thu
2018
PBIO seminar series: Mohan Gupta @ G-328 H.S.B.
Oct 4 @ 9:30 am – 10:30 am
The role of microtubule-generated tension in accurate mitotic chromosome segregation Mohan ‘Moe’ Gupta, Ph.D. Assistant Professor Iowa State University Hosts: Linda Wordeman and Alex Paredez seminar abstract: To ensure genome stability in mitosis, the spindle assembly checkpoint (SAC) delays anaphase if sister chromosomes are not bound to microtubules from opposite spindle poles. Only in this configuration can dynamic microtubules produce tension across sister kinetochores. The interdependency between kinetochore-microtubule attachment and tension has proved challenging to elucidating the role(s) of tension at kinetochores. Thus, whether the SAC responds simply to kinetochore attachment status, or also to tension status remains obscure. Unlike higher eukaryotes, budding yeast kinetochores bind only one microtubule, simplifying the relationship between attachment and tension. To address the role of microtubule-generated tension in checkpoint signaling, we developed a Taxol-sensitive yeast model that allows tension to be reduced by microtubule stabilization in fully assembled spindles with attached kinetochores. Our results reveal that reducing tension on attached kinetochores delays anaphase onset. The tension-specific delay is transient relative to that imposed by kinetochores that are both unattached and tensionless. Furthermore, the mechanism requires only a subset of the core SAC proteins. Our results demonstrate that reduced tension generates a signal to delay anaphase that is temporally and mechanistically distinct from that characterized for unattached kinetochores.
Nov
8
Thu
2018
PBIO seminar series: Ellen Lumpkin @ G-328 H.S.B.
Nov 8 @ 9:30 am – 10:30 am
  Ellen Lumpkin Columbia University   host: John Tuthill
Nov
15
Thu
2018
PBIO seminar series: Daniel Denman @ G-328 H.S.B.
Nov 15 @ 9:30 am – 10:30 am
Correlated spike time variability, population coding, and synchrony in the early visual system. Daniel Denman, PhD Allen Institute host: Adrienne Fairhall   Seminar abstract: In response to repeated presentation of the same stimulus, many visual neurons produce a variable number of spikes. This variability in spike count can be independent, correlated, or anti-correlated between pairs of neurons, and the implications of such correlations on sensory encoding have been extensively explored. In addition, spikes can also occur at variable times within the response (i.e., jitter, or spike time variability). While the magnitude of correlated spike count variability in spike count has been well-studied, the magnitude and sign of correlations in jitter, and any potential implications for visual coding, are not known. In this talk I will present measurements, using high-density electrophysiology (Neuropixels), of correlated jitter within small populations of 20-200 simultaneously recorded neurons across lateral geniculate nucleus and primary visual cortex. I will further discuss proposed mechanisms of correlated jitter and implications for potential and observed synchrony in visual cortical population responses.
Nov
29
Thu
2018
PBIO seminar series: Luke Rice @ HSB G-328
Nov 29 @ 9:30 am – 10:30 am
Dec
6
Thu
2018
PBIO seminar series: EJ Chichilnisky @ G-328 H.S.B.
Dec 6 @ 9:30 am – 10:30 am
EJ Chichilnisky   host: Greg Horwitz
Dec
13
Thu
2018
PBIO seminar series: Michael Long @ G-328 H.S.B.
Dec 13 @ 9:30 am – 10:30 am
seminar title: TBA Michael Long, PhD Associate Professor, Neuroscience and Physiology NYU, School of Medicine host: Adrienne Fairhall
Feb
21
Thu
2019
PBIO seminar series: Carlos Portera-Cailliau @ G-328 H.S.B.
Feb 21 @ 9:30 am – 10:30 am
Dr. Carlos Portera-Cailliau, UCLA   Host: Andres Barria
Mar
21
Thu
2019
PBIO seminar series: Burns C. Blaxall, Ph.D. @ G-328 H.S.B.
Mar 21 @ 9:30 am – 10:30 am
seminar title: TBA Burns C.Blaxall, PhD, FAHA, FACC, FAPS
Director of Translational Science, Heart Institute Director, Center for Translational Fibrosis Research Co-Director, Heart Institute Clinical Research Core & Biorepository
Cincinnati Children’s Hospital Medical Center Professor, UC Department of Pediatrics   host: Chris Liu
Apr
24
Wed
2019
2019 Hille Lecture – Bernardo Sabatini @ TBA
Apr 24 all-day
time: TBD location: TBD Bernardo Sabatini (Harvard Medical School)     host: Stan Froehner
May
16
Thu
2019
PBIO seminar series: Colleen Clancy @ G-328 H.S.B.
May 16 @ 9:30 am – 10:30 am
Colleen Clancy UC Davis   host: Sharona Gordon
May
23
Thu
2019
PBIO seminar series: Rachel Martin @ G-328 H.S.B.
May 23 @ 9:30 am – 10:30 am
What can we learn about protein solubility and aggregation from a cold fish? Rachel Martin Professor Departments of Chemistry and Molecular Biology & Biochemistry UC Irvine host: Sharona Gordon seminar abstract: The βγ-crystallin fold that is ubiquitous in the structural proteins of the vertebrate eye lens is an ancient structural motif found in diverse organisms from all three domains of life. In organisms without eyes, e.g. archaea, bacteria, tunicates, and sponges, βγ-crystallins serve as calcium-binding proteins.  In vertebrates, they are primarily found in the eye lens, where they play an important role in controlling the refractive index gradient of this specialized tissue.  The ubiquitous βγ-crystallins of the vertebrate lens are believed to have descended from an ancestral single-domain Ca2+-binding crystallin by a process that included gene duplication resulting in two copies of the double Greek key domain per chain, as well as selection for high refractive index. Because the lens has negligible protein turnover, the crystallins must remain stable and soluble for the lifetime of the organism despite their extremely high concentrations. In particular, we are interested in the resistance to phase separation of the cold-adapted crystallins of the Antarctic toothfish, Dissostichus mawsoni. The eye lens of D. mawsoni is evolutionarily adapted to function in the permanently sub-freezing waters of the Southern Ocean.  This is in contrast to temperate and tropical fishes, and endothermic mammals, the lenses of which undergo liquid-liquid phase separation at low temperatures.  Mammalian lenses phase separate at temperatures between 10 °C and 20 °C – well above the Antarctic’s sub-zero marine environment.  The ability of the toothfish lens to maintain transparency in this frigid environment is particularly remarkable given that fish lenses have a high concentration of constituent proteins ≥1000 mg * mL-1). Recent work in my group focuses on testing the hypothesis that γ-crystallin isoform heterogeneity coupled with cold selective evolutionary pressures contribute to the clarity of the toothfish lens.  We have measured the thermal stabilities and phase diagrams of seven key γ-crystallin lens proteins, and we are able to control the onset of liquid-liquid phase separation by introducing a small number of surface mutations. The implications of our findings with respect to the roles of frustration, ionic interactions, and protein flexibility liquid-liquid phase separation will be discussed.  
Jun
6
Thu
2019
2019 Crill Lecture – Leslie B. Vosshall @ TBA
Jun 6 – Jun 5 all-day
http://vosshall.rockefeller.edu/ host: Stan Froehner