CALNUC (nucleobindin) is localized in the Golgi apparatus in insect cells

Kawano, Junichi; Kotani, Takuya; Ogata, Yoshikazu; Ohtaki, Sachiya; Takechi, Shinji; Nakayama, Tatsuo; Sawaguchi, Akira; Nagaike, Ryoko; Oinuma, Tsutomu; Suganuma, Tatsuo

doi:10.1078/s0171-9335(04)70024-2

Cited by 25 publications

(16 citation statements)

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“…We investigated the ability of Nucleobindin 1 (NUCB1), a 55-kDa Ca 2+ -binding protein that is widely expressed and is conserved from flies to humans, to inhibit hIAPP fibril formation 21 . We show that a form of NUCB1 engineered to be soluble, s NUCB1, inhibits hIAPP aggregation at sub-stoichiometric levels and effectively disaggregates preformed fibrils in the absence of Ca 2+ .…”

Section: Introductionmentioning

confidence: 99%

Nucleobindin 1 Caps Human Islet Amyloid Polypeptide Protofibrils to Prevent Amyloid Fibril Formation

Gupta

Kapoor

Raleigh

et al. 2012

Journal of Molecular Biology

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Many human diseases are associated with amyloid fibril deposition, including type 2 diabetes mellitus (DM) where human Islet Amyloid Polypeptide (hIAPP) forms fibrils in the pancreas. We report here that engineered, soluble forms of the human Ca2+-binding protein Nucleobindin 1 (NUCB1), prevent hIAPP fibril formation and disaggregate pre-existing hIAPP fibrils. Scanning transmission electron microscopy (STEM) and atomic force microscopy (AFM) indicate that NUCB1 binds to and stabilizes heterogeneous prefibrillar hIAPP species. The NUCB1-stabilized prefibrillar species were isolated by size-exclusion chromatography and analyzed by STEM, dynamic light scattering (DLS) and multi-angle light scattering (MALS). The stabilized prefibrillar species show a size-range of 2–6 million Da and have other similarities to hIAPP protofibrils, but they do not progress to become mature fibrils. The effects of NUCB1 are absent in the presence of Ca2+. We postulate that the engineered forms of NUCB1 prevent hIAPP fibril formation by a mechanism where protofibril-like species are “capped” to prevent further fibril assembly and maturation. This mode of action appears to be different from other protein based inhibitors, suggesting that NUCB1 may offer a new approach to inhibiting amyloid formation and disaggregating amyloid fibrils.

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Section: Introductionmentioning

confidence: 99%

Nucleobindin 1 Caps Human Islet Amyloid Polypeptide Protofibrils to Prevent Amyloid Fibril Formation

Gupta

Kapoor

Raleigh

et al. 2012

Journal of Molecular Biology

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“…Despite these differences in the signal sequence, the two proteins are trafficked to the Golgi apparatus largely due to the inherent hydrophobic nature of their signal sequences (21). Electron microscopy and immunohistochemical studies have revealed the localization of insect calnuc also to the cis-Golgi cisternae and cis-Golgi network, just as observed for human and mouse calnuc (22).…”

Section: Localization Distribution and Expressionmentioning

confidence: 93%

Calnuc: Emerging roles in calcium signaling and human diseases

et al. 2010

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SummaryCalnuc is a recently discovered multidomain protein with EF-hand calcium binding sites. Several studies have reported various interacting partners for calnuc and, therefore, also different sites of localization in the cell. It interacts with important molecules such as DNA, G protein, COX, and amyloid precursor protein among others in addition to being involved in stress response and trafficking. The immense possibilities (of various functions this protein might be involved in) implicate great future in medicine and physiology. Preliminary studies also implicate the possibility of calnuc being involved in some of the human diseases. These initial observations imply the functions that this protein might be involved in. This review emphasizes the importance of further research on this protein. IUBMBIUBMB Life, 62(6): [436][437][438][439][440][441][442][443][444][445][446] 2010

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“…With the exception of calumenin, these proteins have also been found in the lumen of the Golgi cisternae [66]. The Ca 2+ stored in the lumen of the GA is mainly buffered by CALNUC (nucleobindin) [41,67,68], Cab45, the first resident protein described for the Golgi lumen [69,70], and P54/NEFA [71]. CALNUC has also been localized to both the ER and the GA [41,67].…”

Section: Protein Buffers For Ca 2+ In the Lumen Of The Gamentioning

confidence: 96%

The Role of Calcium in Intracellular Trafficking

Micaroni

2010

CMM

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The molecular mechanism of membrane fusion essential to vital cellular activities such as intracellular transport, hormone secretion, enzyme release, or neurotransmission, involve the assembly and disassembly of a specialized set of proteins in opposing bilayers. Recent evidences shed new light on the role Ca(2+) has in the regulation of this mechanism in which the Golgi apparatus works as a central station; from here, Ca(2+) ions are released into and recovered from the cytosol during the different steps of the cargo progression. In fact, transient cytosolic Ca(2+) fluctuations take a crucial role to recruit proteins and enzymes Ca(2+)-sensitive on Golgi membranes where they are involved in membranes remodelling which is fundamental process for the fusion events that allow protein trafficking. Here I provide an overview of the role Ca(2+) plays in intra-Golgi trafficking underlying some interesting aspects to clarify the mechanisms of cargo progression.

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CALNUC (nucleobindin) is localized in the Golgi apparatus in insect cells

Cited by 25 publications

References 0 publications

Nucleobindin 1 Caps Human Islet Amyloid Polypeptide Protofibrils to Prevent Amyloid Fibril Formation

Nucleobindin 1 Caps Human Islet Amyloid Polypeptide Protofibrils to Prevent Amyloid Fibril Formation

Calnuc: Emerging roles in calcium signaling and human diseases

The Role of Calcium in Intracellular Trafficking

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