A combinatorial approach to crystallization of PX–BAR unit of the human Sorting Nexin 9

Pylypenko, Olena; Ignatev, Alexander; Lundmark, Richard; Rasmuson, Erika; Rak, Alexey

doi:10.1016/j.jsb.2007.10.011

Cited by 9 publications

(9 citation statements)

References 18 publications

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“…The BAR-PX domain of SNX9 binds preferentially to membranes of high curvature (15). Indeed, recently it was shown that SNX9 localizes to highly curved regions of late clathrin-coated invaginations, which coincide with PI(4,5)P 2 and PI(3)P (50,51).…”

Section: Discussionmentioning

confidence: 99%

“…Both mechanisms involve the use of bacterial proteins to manipulate essential components of the endocytic machinery, such as the phosphoinositide-converting enzymes that regulate the lipid composition (and hence the curvature) of the PM (9, 10), adaptors and regulators like sorting nexin 9 (SNX9) that control endocytosis and vesicle trafficking (11,12), and finally actin polymerization, which facilitates bacterial uptake (13,14). Interestingly, SNX9 harbors a membrane-curvature-sensing binamphiphysin-rvs (BAR) domain and binds preferentially to membranes of high curvature (15). Using an in vitro system it has been proposed that binding to PI(4,5)P2, the early endosome marker PI(3)P, and domains of high membrane curvature recruits SNX9 in order to trigger the actin machinery and complete endocytosis (16).…”

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confidence: 99%

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Chlamydia-induced curvature of the host-cell plasma membrane is required for infection

Hänsch

Spona

Murra

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

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During invasion of host cells, Chlamydia pneumoniae secretes the effector protein CPn0678, which facilitates internalization of the pathogen by remodeling the target cell’s plasma membrane and recruiting sorting nexin 9 (SNX9), a central multifunctional endocytic scaffold protein. We show here that the strongly amphipathic N-terminal helix of CPn0678 mediates binding to phospholipids in both the plasma membrane and synthetic membranes, and is sufficient to induce extensive membrane tubulations. CPn0678 interacts via its conserved C-terminal polyproline sequence with the Src homology 3 domain of SNX9. Thus, SNX9 is found at bacterial entry sites, where C. pneumoniae is internalized via EGFR-mediated endocytosis. Moreover, depletion of human SNX9 significantly reduces internalization, whereas ectopic overexpression of CPn0678–GFP results in a dominant-negative effect on endocytotic processes in general, leading to the uptake of fewer chlamydial elementary bodies and diminished turnover of EGFR. Thus, CPn0678 is an early effector involved in regulating the endocytosis of C. pneumoniae in an EGFR- and SNX9-dependent manner.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Chlamydia-induced curvature of the host-cell plasma membrane is required for infection

Hänsch

Spona

Murra

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

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“…The protein was crystallized in hanging drops by the vapor diffusion method as described elsewhere (Pylypenko et al , in press). Briefly, in the initial crystallization experiments, the 185 DA‐SNX9 PX‐BAR protein preparation produced a granular crystal like pellet.…”

Section: Methodsmentioning

confidence: 99%

The PX-BAR membrane-remodeling unit of sorting nexin 9

Pylypenko¹,

Lundmark²,

Rasmuson³

et al. 2007

EMBO J

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149

234

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Sorting nexins (SNXs) form a family of proteins known to interact with components in the endosomal system and to regulate various steps of vesicle transport. Sorting nexin 9 (SNX9) is involved in the late stages of clathrin-mediated endocytosis in non-neuronal cells, where together with the GTPase dynamin, it participates in the formation and scission of the vesicle neck. We report here crystal structures of the functional membrane-remodeling unit of SNX9 and show that it efficiently tubulates lipid membranes in vivo and in vitro. Elucidation of the protein superdomain structure, together with mutational analysis and biochemical and cell biological experiments, demonstrated how the SNX9 PX and BAR domains work in concert in targeting and tubulation of phosphoinositide-containing membranes. The study provides insights into the SNX9-induced membrane modulation mechanism.

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“…In addition to the PX domain, SNX9 subfamily members contain an SH3 domain at the N terminus, a low complexity (LC) domain, and a Bin–Amphiphysin–Rvs (BAR) domain at the C terminus (Figure 1A). The PX and BAR domains form a functional unit termed the PX-BAR module that mediates membrane interactions [5,6,7], including membrane deformation [3,4,8]. The BAR domain also mediates homo-dimerization between SNX9 family members [9].…”

Section: Domain Structure and Biochemical Properties Of Snx9mentioning

confidence: 99%

Endocytosis, Metastasis and Beyond: Multiple Facets of SNX9

Bendris

Schmid

2017

Trends in Cell Biology

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Sorting nexin 9 (SNX9) was first discovered as an endocytic accessory protein involved in clathrin-mediated endocytosis. However, recent data suggest that SNX9 is a multifunctional scaffold that coordinates membrane trafficking and remodeling with changes in actin dynamics to affect diverse cellular processes. Here we review the accumulated knowledge on SNX9 with an emphasis on its recently identified roles in clathrin-independent endocytic pathways, cell invasion and cell division, which have implications for SNX9 function in human disease, including cancer.

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A combinatorial approach to crystallization of PX–BAR unit of the human Sorting Nexin 9

Cited by 9 publications

References 18 publications

Chlamydia-induced curvature of the host-cell plasma membrane is required for infection

Chlamydia-induced curvature of the host-cell plasma membrane is required for infection

The PX-BAR membrane-remodeling unit of sorting nexin 9

Endocytosis, Metastasis and Beyond: Multiple Facets of SNX9

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