A short carboxy-terminal domain of polycystin-1 reorganizes the microtubular network and the endoplasmic reticulum

Gao, Hongyu; Sellin, Lorenz; Pütz, Michael; Nickel, Christian H.; Imgrund, Michael; Gerke, Peter; Nitschke, Roland; Walz, Gerd; Kramer-Zucker, Albrecht

doi:10.1016/j.yexcr.2009.01.027

Cited by 9 publications

(7 citation statements)

References 61 publications

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“…As CLIMP-63 and Syn5 interact with each other, and both bind MTs, it is tempting to speculate that multivalent and cooperative interactions between ER membrane proteins and MTs are required for the organization of the rough ER, as in the case of the organization of the tubular ER network (Park et al, 2010). In this context, it is interesting that the overexpression of the C-terminal region of polycystin 1 causes ER-MT rearrangement (Gao et al, 2009). Polycystin 1 is known to form a heterodimer with polycystin 2 (Qian et al, 1997;Tsiokas et al, 1997), which has been reported to interact with Syn5 (Geng et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Contribution of the long form of syntaxin 5 to the organization of the endoplasmic reticulum

Miyazaki

Wakana

Noda

et al. 2012

Journal of Cell Science

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SummaryThe SNARE protein syntaxin 5 exists as long (42 kDa) and short (35 kDa) isoforms. The short form is principally localized in the Golgi complex, whereas the long form resides not only in the Golgi but also in the endoplasmic reticulum (ER). Although the Golgi-localized short form has been extensively investigated, little is known about the long form. In the present study, we demonstrate that the long form of syntaxin 5 functions to shape the ER. We found that overexpression of the long form of syntaxin 5 induces rearrangement and coalignment of the ER membrane with microtubules, the pattern of which is quite similar to that observed in cells overexpressing CLIMP-63, a linker between the ER membrane and microtubules. The ability of syntaxin 5 to induce ER-microtubule rearrangement is not related to its SNARE function, but correlates with its binding affinities for CLIMP-63, and CLIMP-63 is essential for the induction of this rearrangement. Microtubule co-sedimentation assays demonstrated that the long form of syntaxin 5 has a substantial microtubulebinding activity. These results suggest that the long form of syntaxin 5 contributes to the regulation of ER structure by interacting with both CLIMP-63 and microtubules. Indeed, depletion of syntaxin 5 caused the spreading of the ER to the cell periphery, similar to the phenotype observed in cells treated with the microtubule-depolymerizing reagent nocodazole. Our results disclose a previously undescribed function of the long form of syntaxin 5 that is not related to its function as a SNARE.

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Section: Discussionmentioning

confidence: 99%

Contribution of the long form of syntaxin 5 to the organization of the endoplasmic reticulum

Miyazaki

Wakana

Noda

et al. 2012

Journal of Cell Science

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“…The ER is emerging as a common target for PKD susceptibility gene products. Recent data indicate PKD1 influences the shape and localization of both the microtubule network and the ER (Gao et al , 2009), and PKD2 is an abundant ER protein that functions as a novel intracellular Ca 2+ release channel (Koulen et al , 2002; Li et al , 2005). …”

Section: Discussionmentioning

confidence: 99%

Autosomal Recessive Polycystic Kidney Disease Epithelial Cell Model Reveals Multiple Basolateral Epidermal Growth Factor Receptor Sorting Pathways

Ryan¹,

Verghese

Cianciola³

et al. 2010

MBoC

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“…Though many aspects of the regulation PC2 function remain unclear, the growing evidence of its multiple interactions with cytoskeleton organizing proteins supports its Ca 2+ -dependent mechanosensorial role at different cellular compartments (for a comprehensive review see references 15, 20, 21). Interestingly, the subcellular localization of PC1 at the cell adherens, desmosomes, focal adhesions, and cilia provides the proximity with cytoskeletal components suggesting a possible role of PC1 in the control of cytoskeleton rearrangement (Figure1) [22-25]. …”

Section: Introductionmentioning

confidence: 99%

Cilium, centrosome and cell cycle regulation in polycystic kidney disease

Lee¹,

Battini²,

Gusella³

2011

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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Polycystic kidney disease is the defining condition of a group of common life-threatening genetic disorders characterized by the bilateral formation and progressive expansion of renal cysts that lead to end stage kidney disease. Although a large body of information has been acquired in the past years about the cellular functions that characterize the cystic cells, the mechanism(s) triggering the cystogenic conversion are just starting to emerge. Recent findings link defects in ciliary functions, planar cell polarity pathway, and centrosome integrity in early cystic development. Many of the signals dysregulated during cystogenesis may converge on the centrosome for its central function as a structural support for cilia formation and a coordinator of protein trafficking, polarity, and cell division. Here, we will discuss the contribution of proliferation, cilium and planar cell polarity to the cystic signal and will analyze in particular the possible role that the basal bodies/centrosome may play in the cystogenetic mechanisms.

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A short carboxy-terminal domain of polycystin-1 reorganizes the microtubular network and the endoplasmic reticulum

Cited by 9 publications

References 61 publications

Contribution of the long form of syntaxin 5 to the organization of the endoplasmic reticulum

Contribution of the long form of syntaxin 5 to the organization of the endoplasmic reticulum

Autosomal Recessive Polycystic Kidney Disease Epithelial Cell Model Reveals Multiple Basolateral Epidermal Growth Factor Receptor Sorting Pathways

Cilium, centrosome and cell cycle regulation in polycystic kidney disease

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