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Mable Lam

As seen in: Nature, BioRxiv, Cell Press
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Articles by Mable Lam

Neuroligin-3–CSPG4 interaction maintains oligodendrocyte precursor cell progenitor state and promotes glioma proliferation through mechanotransduction

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By Yoon Seok Kim, Shawn M. Gillespie, Anna C. Geraghty, Belgin Yalçın, Aerin Yang, Rebecca Mancusi, Jared D. Hysinger, James Reed, Richard Drexler, Michael A. Quezada, Karen Malacon, Pamelyn J. Woo, Youkyeong Gloria Byun, Christopher W. Mount, Mable Lam, J. Bradley Zuchero, Jacqueline Trotter, Michelle Monje, Alexis English Ivec
| Nature Verified
Abstract Glioma pathophysiology is robustly regulated by interactions with neurons. Key to these interactions is the role of neuroligin-3 (NLGN3), a synaptic adhesion molecule shed in response to neuronal activity that functions as a paracrine factor crucial for glioma growth. Here we elucidate the mechanistic pathway whereby shed NLGN3 interacts with glioma and their normal glial counterparts.
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pHusion: A robust and versatile toolset for automated detection and analysis of exocytosis

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By Ellen C O'Shaughnessy, Mable Lam, Samantha E. Ryken, Theresa Wiesner
| BioRxiv
Abstract Exocytosis is a fundamental process used by eukaryotic cells to regulate the composition of the plasma membrane and facilitate cell-cell communication. To investigate the role exocytosis plays in neuronal morphogenesis, previously we developed computational tools with a graphical user interface (GUI) to enable the automatic detection and analysis of exocytic events (ADAE GUI) from fluorescence timelapse images.
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pHusion: A robust and versatile toolset for automated detection and analysis of exocytosis

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By Ellen C O’Shaughnessy, Mable Lam, Theresa Wiesner, Samantha E. Ryken
| BioRxiv
Thank you for your interest in spreading the word about bioRxiv. NOTE: Your email address is requested solely to identify you as the sender of this article. Your Email * Your Name * Send To * Enter multiple addresses on separate lines or separate them with commas. Message Subject (Your Name) has forwarded a page to you from bioRxiv Message Body (Your Name) thought you would like to see this page from the bioRxiv website.
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Misfolded proteins bind and activate death receptor 5 to trigger apoptosis during unresolved endoplasmic reticulum stress

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By Mable Lam, Avi Ashkenazi, Peter Walter, Scot A Marsters
| eLife
Abstract Disruption of protein folding in the endoplasmic reticulum (ER) activates the unfolded protein response (UPR)—a signaling network that ultimately determines cell fate. Initially, UPR signaling aims at cytoprotection and restoration of ER homeostasis; that failing, it drives apoptotic cell death.
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The Mars1 kinase confers photoprotection through signaling in the chloroplast unfolded protein response

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By Masakazu Iwai, Peter Walter, Karina Perlaza, Hannah Toutkoushian, Morgane Boone, Mable Lam, Martin C Jonikas, Silvia Ramundo
| eLife
Abstract In response to proteotoxic stress, chloroplasts communicate with the nuclear gene expression system through a chloroplast unfolded protein response (cpUPR). We isolated Chlamydomonas reinhardtii mutants that disrupt cpUPR signaling and identified a gene encoding a previously uncharacterized cytoplasmic protein kinase, termed Mars1—for mutant affected in chloroplast-to-nucleus retrograde signaling—as the first known component in cpUPR signal transmission.
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