Publications by authors named "N L Tjandra"
Tsg101 mimicry of canonical E2 enzymes underlies its role in ubiquitin signaling.
Proc Natl Acad Sci U S A
January 2025
Tsg101 is a highly conserved protein best known as an early-functioning component of cellular ESCRT machinery participating in recognition, sorting, and trafficking of cellular cargo to various intracellular destinations. It shares sequence and structural homology to canonical ubiquitin-conjugating (E2) enzymes and is linked to diverse events regulated by Ub signaling. How it might fulfill these roles is unclear.
View Article and Find Full Text PDFWe recently identified N-cadherin as a novel receptor for fibrin and localized complementary binding sites within the fibrin βN-domains and the third and fifth extracellular domains (EC3 and EC5) of N-cadherin. We also hypothesized that the His16 and Arg17 residues of the βN-domains and the (Asp/Glu)-X-(Asp/Glu) motifs present in the EC3 and EC5 domains may play roles in the interaction between fibrin and N-cadherin. The primary objectives of this study were to test these hypotheses and to further clarify the structural basis for this interaction.
View Article and Find Full Text PDFArticle Synopsis
- Tsg101 is a protein critical for cellular processes related to transport, specifically involved in recognizing tagged proteins and recruiting other necessary components for transport, particularly during virus budding.* -
- The study highlights how Tsg101 interacts with ubiquitin (Ub) ligases (E3 enzymes), revealing that disrupting a specific motif in Tsg101 shifts the budding process’s dependency to another ligase, Nedd4L, showing the intricate interplay between these proteins.* -
- Small molecule experiments showed that disrupting Tsg101’s ability to bind Ub or Nedd4 halted viral budding early in the process, emphasizing Tsg101's role in regulating E3 ligases and its importance in viral particle assembly and overall cellular functions.*
Article Synopsis
- Microtubule function is influenced by the "tubulin code," which includes various posttranslational modifications, particularly glutamylation, a common modification where branched glutamate chains are added.
- Glutamylation is regulated by specific enzymes that add and remove these chains, and maintaining this balance is crucial for cell health; mutations in enzymes can lead to diseases.
- The study presents detailed structures of the glutamylation eraser enzyme CCP5 bound to microtubules, revealing how it identifies and processes glutamate branches, which is essential for understanding tubulin modification and its role in cellular functions.
The odorant binding protein, OBP44a is one of the most abundant proteins expressed in the brain of the developing fruit fly Drosophila melanogaster. Its cellular function has not yet been determined. The OBP family of proteins is well established to recognize hydrophobic molecules.
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