Ee Ling Ng

National University of Singapore

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Bor Luen Tang

National University of Singapore

Ya Wang

Wenzhou Medical University

Jun Jie Ng

National University of Singapore

Ting Wang

Xinjiang Academy of Agricultural and Reclamation Science

Fengyi Liang

National University of Singapore

Anchen Guo

Capital Medical University

Ya Wang

Lanzhou University of Technology

Kooi Hoong Chong

National University of Singapore

Bin Gan

Chinese Academy of Surveying and Mapping

Selina Aulia

National University of Singapore

Cooperative Institutions

National University of Singapore

National University Health System

Guangzhou Medical University

Guangdong Medical College

Nanjing Drum Tower Hospital

University Health System

Institute of Molecular and Cell Biology

National University Heart Centre Singapore

SingHealth Polyclinics

Defence Science and Technology Agency

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Rab22B’s role in trans-Golgi network membrane dynamics

Biochemical and Biophysical Research Communications (2007)

Ee Ling Ng Ya Wang Bor Luen Tang

Dynamics

Golgi membrane

10.1016/j.bbrc.2007.07.076

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Citations (34)

Rabs and cancer cell motility

Cell Motility and the Cytoskeleton (2009)

Bor Luen Tang Ee Ling Ng

Abstract The Rab family of small GTPases functions in regulating vesicular transport in all eukaryotes. In the past few years, several important reports have linked some members of the Rab family to intriguing mechanistic aspects of cancer cell migration and invasiveness. Rab5 and Rab21 associate with α‐integrin subunits and modulate their endosomal traffic and subcellular localization. Expression of the latter enhances adhesion and migration of certain cancer cell types. Rab25 has been functionally linked to tumor progression and the invasiveness of some epithelial cancers. Rab25 promotes invasive migration of cells in three‐dimensional microenvironments by associating with α5β1 integrin, and directing its recycling to dynamic ruffling protrusions at the migrating cell front. Acting directly, or through its effector, the Rab‐coupling protein, Rab25 could potentially engage both integrin and epidermal growth factor receptor and enhance their oncogenic recycling and signaling. Tumor invasiveness may also be modulated by Rab8‐mediated exocytic traffic of MT1‐matrix metalloproteinase, with the latter's activity likely influenced by interaction with the mammalian suppressor of Sec4 (Mss4), a Rab8 guanine nucleotide exchange factor, and integrin. We discuss highlights in the recent literature that point towards a role for Rab‐mediated membrane traffic in cancer cell migration and invasion. Cell Motil. Cytoskeleton 2009. © 2009 Wiley‐Liss, Inc.

Rab

Membrane ruffling

Cell polarity

10.1002/cm.20376

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Rab22B is expressed in the CNS astroglia lineage and plays a role in epidermal growth factor receptor trafficking in A431 cells

Journal of Cellular Physiology (2009)

Ee Ling Ng Jun Jie Ng Fengyi Liang Bor Luen Tang

The expression profile and functions of the brain-enriched Rab22B/Rab31 small GTPase had remained uncharacterized. Using specific antibodies against Rab22B, we found the protein to be exceptionally enriched in nestin and RC2-positive radial glia of the embryonic mouse brain. In the adult brain, Rab22B is rather specifically expressed in glial fibrillary acidic protein (GFAP)-positive mature astrocytes, but is not clearly detectable in either 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase)-positive mature oligodendrocytes or betaIII-tubulin (TuJ)-positive neurons. In probing for specific functions of Rab22B, we found that Rab22B silencing in A431 cells resulted in abnormal trafficking of the epidermal growth factor receptor (EGFR), Texas-red-labeled EGF, and the cation-independent mannose 6-phosphate receptor (M6PR). Affinity pull-down assays and co-immunoprecipitation analysis indicated that Rab22B could associate with EGFR in a GTP-dependent manner. Rab22B is thus a Rab protein specifically expressed in the astroglia lineage and may have a role in regulating EGFR trafficking in some cell types. Given that EGFR signaling modulates astrocyte development and oncogenesis of multiple cell types, Rab22B may thus have specific developmental or pathophysiological roles in cell types which it is enriched in.

Nestin

10.1002/jcp.21911

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Citations (26)

Open brain gene product Rab23: Expression pattern in the adult mouse brain and functional characterization

Journal of Neuroscience Research (2006)

Anchen Guo Ting Wang Ee Ling Ng Selina Aulia Kooi Hoong Chong

Abstract The gene mutated in the mouse open brain ( opb ) phenotype antagonizes sonic hedgehog ‐mediated signaling and encodes a small GTPase of the Rab family, Rab23. To date, the brain expression profile and exact mechanism of function of the Rab23 protein has remained unknown. Specific antibodies generated against Rab23 showed that the protein is highly enriched in the adult rodent brain and present in low levels in multiple tissues of the adult rodent. Rab23 is found in the cytosol as well as being associated with the plasma and endosomal membranes. In the adult mouse brain, Rab23 is found in βIII tubulin (TuJ) positive neuronal cell bodies and are most prominent in the cortex, hypothalamus and the cerebellum. It is, however, absent from glial fibrillary acidic protein (GFAP) positive astrocytes or CNPase positive oligodendrocytes. Despite the plasma membrane/endosomal membrane localization of Rab23, neither overexpression of the GTP‐restricted nor the GDP‐bound mutant forms affect internalization of transferrin or epidermal growth factor. Exogenous overexpression of Rab23 or its mutants also did not affect the morphological differentiation of thalamic neurons in culture. Expression of Rab23 in the adult brain is suggestive, however, of having a postnatal function beyond its role in embryonic development. © 2006 Wiley‐Liss, Inc.

Rab

10.1002/jnr.20788

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Rab GTPases and their roles in brain neurons and glia

Brain Research Reviews (2008)

Ee Ling Ng Bor Luen Tang

Rab

Neurite

Small GTPase

Synaptic vesicle recycling

Axoplasmic transport

10.1016/j.brainresrev.2008.04.006

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Citations (150)

Rab23: What Exactly Does it Traffic?

Traffic (2006)

Ya Wang Ee Ling Ng Bor Luen Tang

Rab23 is the product of the gene mutated in the mouse open brain1 phenotype, which displays neural tube defects. It appears to antagonize sonic hedgehog (Shh) ‐mediated signaling during mouse development, presumably by regulating the intracellular trafficking of one or more of Shh's‐signaling components. The Shh receptor Patched1 (Ptch1) and its downstream effector Smoothened (Smo) were initial prime suspects as they are membrane proteins whose cellular dynamics are modulated by the Shh signal. However, Rab23 mutants do not appear to affect the localization and dynamics of either protein. Genetic analyses have now shown that Rab23 functions downstream of Smo and affects the function of the Shh‐regulated Gli family of transcription factors in a more direct manner than previously thought. A plethora of proteins that influence Shh signaling and whose cellular trafficking could potentially be regulated by Rab23 has also emerged. These include members of the intraflagellar transport complex, as well as motor proteins responsible for their assembly at the cilia. Rab23 is also expressed in adult mouse neurons and may thus have functions beyond embryonic developmental stages and Shh signaling. We discuss these new findings and explore the myriad of possibilities whereby Rab23 may function.

10.1111/j.1600-0854.2006.00416.x

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Rab GTPases regulating receptor trafficking at the late endosome–lysosome membranes

Cell Biochemistry and Function (2012)

Ee Ling Ng Bin Gan Fanny Ng Bor Luen Tang

Lysosomes serve key degradative functions for the turnover of membrane lipids and protein components. Its biogenesis is principally dependent on exocytic traffic from the late endosome via the trans-Golgi network, and it also receives cargo to be degraded from the endocytic pathway. Membrane trafficking to the late endosome-lysosome is tightly regulated to maintain the amplitude of signalling events and cellular homeostasis. Key coordinators of lysosomal traffic include members of the Rab small GTPase family. Amongst these, Rab7, Rab9 and the more recently studied Rab22B/31 have all been reported to regulate membrane trafficking processed at the late endosome-lysosome system. We discuss what is known about the roles of these Rab proteins and their interacting partners on the regulation of traffic of important receptor proteins such as the epidermal growth factor receptor (EGFR) and the mannose 6-phosphate receptor (M6PR), in association with the late endosome-lysosome system. Better knowledge of EGFR and M6PR traffic in this regard may aid in understanding the pathological processes, such as oncogenic transformations associated with these receptors.

Rab

Mannose 6-phosphate receptor

10.1002/cbf.2827

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Citations (36)