A family of proteins involved in intracellular transport

Aalto, Markku K.; Keränen, Sirkka; Ronne, Hans

doi:10.1016/0092-8674(92)90462-l

Cited by 77 publications

(52 citation statements)

References 13 publications

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“…They are thought to interact via the coiled-coil domains predicted from their sequences (Chapman et al, 1994;Hayashi et al, 1994). Assembly of the SNARE complex is regulated by the Secl/Slyl family of proteins (Aalto et al, 1991;Dascher et al, 1991;Ossig et al, 1991;Aalto et al, 1992;Pevsner, 1996) and the Ypt/Rab family of small GTPbinding proteins (Salminen and Novick, 1987;Segev et al, 1988;Novick and Brennwald, 1993;Pfeffer, 1994). The cognate SNARE complex acts as a scaffold for the binding of the ATPase NSF via the soluble NSF attachment proteins (SNAPs) (Sollner et al, 1993b).…”

Section: Introductionmentioning

confidence: 99%

An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal.

Hui

Nakamura

Sonnichsen

et al. 1997

MBoC

124

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The early Golgi t-SNARE (target-membrane-associated soluble-N-ethylmaleimide-sensitive factor attachment protein receptor) syntaxin 5 is thought to specify the docking site for both COPI and COPII coated vesicles originating from the endoplasmic reticulum (ER) and COPI vesicles on the retrograde pathway. We now show that there are two forms of syntaxin 5 that appear to be generated from the same mRNA by alternative initiation of translation. The short form (35 kDa) corresponds to the published sequence. The long form (42 kDa) has an N-terminal cytoplasmic extension containing a predicted type II ER retrieval signal. When grafted onto a reporter molecule, this signal localized the construct to the ER. Biochemical fractionation and immunofluorescence microscopy showed that there was less of the long form in the Golgi apparatus and more in peripheral punctate structures, some of which colocalized with markers of the intermediate compartment. The predicted absence of the long form in budding yeast points to a function unique to higher organisms.

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Section: Introductionmentioning

confidence: 99%

An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal.

Hui

Nakamura

Sonnichsen

et al. 1997

MBoC

124

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“…SEC1 is a hydrophilic protein required for proper transport from the Golgi to the plasma membrane (27). SEC1 is itself a member of a family of proteins involved in membrane trafficking (28). SLY1 (19) and SLP1 (29), two proteins with sequence similarity to SEC1, are required for transport from the ER to the Golgi and from the Golgi to the vacuole, respectively.…”

Section: Introductionmentioning

confidence: 99%

The molecular machinery for secretion is conserved from yeast to neurons.

Bennett

Scheller

1993

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

583

230

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A variety of approaches have been utilized to identify and characterize the molecules that mediate vesicular trafficking along the secretory pathway. Two approaches that have been particularly fruitful include the genetic dissection of the yeast secretory pathway and the biochemical characterization of proteins involved in the synaptic vesicle membrane trafficking in the mammalian nerve terminal. The recent convergence of these approaches suggests that common mechanisms may underlie a wide variety of vesicle-mediated transport steps. We discuss the results that support this possibility and propose a model for synaptic vesicle docking and fusion that incorporates evolutionarily conserved elements that may be part of a constitutive fusion machinery and specialized elements that may mediate regulatory events that are specific to the process of neurotransmitter release.

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“…These three ER-Golgi v-SNAREs interact with the t-SNARE Sed5p, which has been localized to the cis side of the Golgi stack in animal cells (30,31). Formation of v-t-SNARE complexes is tightly regulated and controlled by several proteins, including small GTP binding proteins belonging to the Rab family and members of the Sec1p protein family (19,(32)(33)(34)(35). v-t SNARE complexes do not form when these proteins or the SNAREs themselves are inactivated (36 -38).…”

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confidence: 99%

Ykt6p, a Prenylated SNARE Essential for Endoplasmic Reticulum-Golgi Transport

McNew¹,

Søgaard²,

Lampen³

et al. 1997

Journal of Biological Chemistry

224

220

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Vesicular transport between secretory compartments requires specific recognition molecules called SNAREs. Here we report the identification of three putative SNAREs, p14 (Sft1p), p28 (Gos1p), and a detailed characterization of p26 (Ykt6p). All three were originally isolated as interacting partners of the cis Golgi target membrane-associated SNARE Sed5p, when Sec18p (yeast NSF) was inactivated. YKT6 is an essential gene that codes for a novel vesicle-associated SNARE functioning at the endoplasmic reticulum-Golgi transport step in the yeast secretory pathway. Depletion of Ykt6p results in the accumulation of the p1 precursor (endoplasmic reticulum form) of the vacuolar enzyme carboxypeptidase Y and morphological abnormalities consistent with a defect in secretion. Membrane localization of Ykt6p is essential for protein function and is normally mediated by isoprenylation. However, replacement of the isoprenylation motif with a bona fide transmembrane anchor results in a functional protein confirming that membrane localization, but not isoprenylation per se, is required for function. Ykt6p and its homologues are highly conserved from yeast to human as demonstrated by the functional complementation of the loss of Ykt6p by its human counterpart. This is the first example of a human SNARE protein functionally replacing a yeast SNARE. This observation implies that the specific details of the vesicle targeting code, like the genetic code, are conserved in evolution.

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A family of proteins involved in intracellular transport

Cited by 77 publications

References 13 publications

An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal.

An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal.

The molecular machinery for secretion is conserved from yeast to neurons.

Ykt6p, a Prenylated SNARE Essential for Endoplasmic Reticulum-Golgi Transport

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