Membrane Trafficking | Health & Disease
“Membrane Contact Sites: Methodology, Biology & Pathology”28 September – 03 October 2025 | Monopoli (BA), Italyhttps://meetings.embo.org/event/25-membrane-contacts Gordon Research Conference “Membranes as Drivers of Cellular and Organismal Processes”July
Yaron Vinik, Avi Maimon, Vinay Dubey, Harsha Raj, Ifat Abramovitch, Sergey Malitsky, Maxim Itkin, Avi Ma’ayan, Frank Westermann, Eyal Gottlieb, Eytan Ruppin, and Sima Lev.
A presentation from Sima Lev about the lipid transfer proteins in cancer.
The annual clinical research conference in Israel will be held on February 3 at the David Intercontinental Hotel in Tel Aviv. Attached are the lecture
Weizmann Institute of Science has a new President, and Professor Sima Lev sends her congratulations: “Congratulation to Prof. Alon Chen, the new President of the Weizmann
The Biochemical Society had a great meeting on the 21-24 of October in Turin, Italy. The subject of the meeting this year was: Cell Signaling
Senior author Sima Lev says this probably allows the two transport steps to be coordinated. She now wants to investigate whether COG subunits interact with
Prof. Sima Lev and her student Orly Laufman revealed how a membrane-tethering complex promotes the transport of vesicles from endosomes to the trans-Golgi network (TGN).
Prof. Sima Lev and her team identified a unique direct interaction between Cog4 and the SM protein Sly. Link Laufman et al., EMBO J. 2009.
The octameric COG complex (Cog1–8), regulates intra-Golgi and endosome-to-Golgi retrograde transport, interact with the SNARE motifs of multiple Golgi SNAREs. Prof. Sima Lev extensively studied
Multisubunit tethering complexes (MTCs) interact with soluble SNAREs to couple vesicular tethering with fusion. Conserved Oligomeric Golgi (COG) and Golgi-associated retrograde protein (GARP) MTCs interact
Tethering factors are a large group of proteins or multiple-protein complexes that link transport vesicles to their cognate target membranes. Tethering factors can be divided
Schematic summary of known mammalian SNARE complexes and their sites of action along the exocytic and endocytic pathways. Potential v-SNAREs are indicated in red; the
The SNARE hypothesis was first introduced in 1993 and suggested that a v-SNARE on the vesicle pairs with cognate t-SNAREs on the target membrane to
The fusion of two membrane compartments into a single continuous bilayer is fundamental for diverse biological processes including bacterial reproduction, gametes fertilization, virus internalization, and
Nir2, CERT and OSBP are three lipid-transfer proteins containing an FFAT motif, interact with VAP-A/B and localize to the Golgi apparatus at steady-state. Targeting of
Potential mechanisms underlying the aggregation and motor neurodegeneration of VAP-B(P56S) mutant. The Lev’s lab found that the P56S mutation enhances the exposure of hydrophobic patches
Oligomerization and conformational changes within the MSP are required for VAP-B(P56S) aggregation and neurotoxicity
Multilamellar ER-derived membrane structures called ‘Karmellea’ were associated with VAP-B(P56S) as reported by Gkogkas et al., J. Neurochem. 2011
Prof. Sima Lev’ team showed that the three Nir proteins interact with VAP-B, but each interaction affects the structural integrity of the ER membranes differently.
Prof. Sima Lev’ team showed that the Nir2 protein mainly localizes to the Golgi in interphase cells, and isolated the integral ER-membrane protein VAP-B as
The Nir/rdgB family of proteins has been identified in a variety of eukaryotic organisms, ranging from worms to mammals. The Drosophila retinal degeneration B (rdgB),
The Nir Proteins Family, Nir2 functions at ER-Golgi MCSs, Co-expression of Nirs with VAPs distinctly affects the ER morphology.
To demonstrate the correlation between aggregate formation and cell viability, we compared the effect of VAP-B(WT), the P56S mutant, and the P56S/DCC/II mutant on Neuro2a
Characterization of p56S insoluble aggregates. Analysis of the solubilization of the indicated mutants suggest that the oligomerization of VAP-B(P56S) is mediated mainly by the coiled-coil
Oligomerization of VAP-B(P56S) prevents binding of FFAT proteins. We found that the conformational changes of MSP domain of P56S mutant have no direct effect on
The P56S mutation induces the exposure of hydrophobic patches, thereby facilitating MSP oligomerization. To better understand how the P56S mutation enhances oligomerization of VAP-B(P56S), we
The N-terminal cytoplasmic MSP (major sperm protein) domain of VAP-B consistes of 125 amino acids (aa), and a coiled-coil domain (CCD) of ~50 aa. Proline
We defined the structural requirements for VAP-B oligomerization and demonstrated their contribution for VAP-B(P56S) aggregation and neurotoxicity. We show that the oligomerization of VAP-B is
Potential mechanisms underlying the aggregation and motor neurodegeneration of VAP-B (P56S) mutant.
Expression of the VAP-B(P56S) mutant in cultured cells results in the formation of insoluble protein aggregates. These aggregates might induce loss-of-function of wild-type VAP-B protein, gain of toxic
The VAP-B is an integral endoplasmic reticulum (ER)-membrane protein implicated in the regulation of a wide range of cellular processes, including membrane trafficking, lipid transport and metabolism,
Amyotrophic lateral sclerosis (ALS) is a motor neurone disease (MND) characterized by death of motor neurons in the cerebral cortex, brain stem, and spinal cord. ALS is one
The Golgi apparatus (discovered by Camillo Golgi), is the central organelle of the secretory pathway, involved in the post-translational modification of many cellular proteins and lipids
Read the presentation: Prof. Sima Lev – The role of Nir proteins in phosphatidylinositol (PI) transport and beyond from Sima Lev
The VAPs (VAMP-associated proteins) are highly conserved integral endoplasmic reticulum (ER)-membrane proteins, implicated in diverse cellular functions, including regulation of lipid transport and homeostasis, membrane
Membrane trafficking pathways are mediated by a network of proteins and lipids that coordinately function to efficiently and rapidly transport lipids, secreted, luminal and integral