Viki Allan

Motor proteins: A dynamic duo

The interactions between the microtubule motor cytoplasmic dynein and its putative regulator dynactin have been shown to be dynamic and complex.

Involvement of β-COP in membrane traffic through the Golgi complex

Abstract Non-clathrin-coated vesicles mediate membrane traffic through the Golgi complex. The proteins that constitute the coats of these vesicles have similar molecular weights to the clathrin coat proteins. A major component of the coat of non-clathrin-coated vesicles, β-COP, has significant homology with the clathrin coat protein β-adaptin, indicating that the coats of the two different classes of vesicles may be structurally and functionally homologous.

Molecular motors and the Golgi complex: Staying put and moving through

The Golgi apparatus is a highly dynamic organelle through which nascent proteins released from the endoplasmic reticulum (ER) are trafficked. Proteins are post-translationally modified within the Golgi and subsequently packaged into carriers for transport to a variety of cellular destinations. This transit of proteins, as well as the maintenance of Golgi structure and position, is highly dependent upon the actin and microtubule cytoskeletons and their associated molecular motors. Here we review how motors contribute to the correct functioning of the Golgi in higher eukaryotes and discuss the secretory pathway as a model system for studying cooperation between motor proteins.

Intermediate Filaments: Vimentin Moves in

Vimentin intermediate filaments move bi-directionally along microtubules in the cell. Recent work has identified the microtubule motor cytoplasmic dynein as the missing inward-directed motor that drives this movement.

Membrane traffic motors.

There is a wealth of data suggesting that microtubules and associated motor proteins play important roles in orchestrating membrane traffic within higher eukaryotes, with myosins and actin filaments fulfilling similar functions in organisms such as fungi, algae and plants. In addition, evidence is accumulating that both cytoskeletal systems can co‐operate within one cell. Recent studies have highlighted how individual motor proteins can act at multiple steps in the membrane‐traffic pathways, and in contrast, how more than one motor type may be involved in each transport step and in generating organelle morphology.

N‐Terminal Kinesins: Many and Various

Molecular motors are a fascinating group of proteins that have vital roles in a huge variety of cellular processes. They all share the ability to produce force through the hydrolysis of adenosine triphosphate, and fall into classes groups: the kinesins, myosins and the dyneins. The kinesin superfamily itself can be split into three major groups depending on the position of the motor domain, which is localized N‐terminally, C‐terminally, or internally. This review focuses on the N‐terminal kinesins, providing a brief overview of their roles within the cell, and illustrating recent key developments in our understanding of how these proteins function.

How and why does the endoplasmic reticulum move

The ER (endoplasmic reticulum) is a fascinating organelle that is highly dynamic, undergoing constant movement and reorganization. It has many key roles, including protein synthesis, folding and trafficking, calcium homoeostasis and lipid synthesis. It can expand in size when needed, and the balance between tubular and lamellar regions can be altered. The distribution and organization of the ER depends on both motile and static interactions with microtubules and the actin cytoskeleton. In the present paper, we review how the ER moves, and consider why this movement may be important for ER and cellular function.

Organelle Movement: Dynactin: portrait of a dynein regulator

Recent studies of dynactin, a protein complex implicated in regulating the cytoplasmic motor protein dynein, reveal that the complex contains a specialized actin filament and may also interact with microtubules.

Phosphorylation of p97(VCP) and p47 in vitro by p34cdc2 kinase.

The hexameric ATPase p97/yeast Cdc48p has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation. p97/Cdc48p contains two conserved consensus p34cdc2 kinase phosphorylation sites within its second ATP binding domain. This domain is likely to play a role in stabilising the hexameric form of the protein. We therefore investigated whether p97 could be phosphorylated by p34cdc2 kinase in vitro, and whether phosphorylation might influence the oligomeric status of p97. Monomeric, but not hexameric, p97 was phosphorylated by p34cdc2 kinase, as was the p97-associated protein p47. However, phosphorylation by p34cdc2 kinase did not impair subsequent re-hexamerisation of p97, implying that the phosphorylated residue(s) are not critical for interaction between p97 monomers. Moreover, p97 within both interphase and mitotic cytosols was almost exclusively hexameric, suggesting that the activity of p97 is not regulated during mitosis by influencing the extent of oligomerisation.

Cell cycle regulation of organelle transport.

Microtubule- and actin-based motors play a wide range of vital roles in the organisation and function of cells during both interphase and mitosis, all of which are likely to be under strict control. Here, we describe how one of these roles--the movement of membranes--is regulated through the cell cycle. Organelle movement in many species is greatly reduced in mitosis as compared to interphase, and this change occurs concomitantly with an inhibition of most membrane traffic functions. Data from in vitro studies is shedding light on how microtubule motor regulation may be achieved.